LIVIVO - Search results -

Search results

Result 1 - 10 of total 74

Search options

Article: ALS2-Related Motor Neuron Diseases: From Symptoms to Molecules

Miceli, Marcello / Exertier, Cécile / Cavaglià, Marco / Gugole, Elena / Boccardo, Marta / Casaluci, Rossana Rita / Ceccarelli, Noemi / De Maio, Alessandra / Vallone, Beatrice / Deriu, Marco A.

Biology. 2022 Jan. 05, v. 11, no. 1

2022

Abstract: Infantile-onset Ascending Hereditary Spastic Paralysis, Juvenile Primary Lateral Sclerosis and Juvenile Amyotrophic Lateral Sclerosis are all motor neuron diseases related to mutations on the ALS2 gene, encoding for a 1657 amino acids protein named Alsin. ...

Abstract	Infantile-onset Ascending Hereditary Spastic Paralysis, Juvenile Primary Lateral Sclerosis and Juvenile Amyotrophic Lateral Sclerosis are all motor neuron diseases related to mutations on the ALS2 gene, encoding for a 1657 amino acids protein named Alsin. This ~185 kDa multi-domain protein is ubiquitously expressed in various human tissues, mostly in the brain and the spinal cord. Several investigations have indicated how mutations within Alsin’s structured domains may be responsible for the alteration of Alsin’s native oligomerization state or Alsin’s propensity to interact with protein partners. In this review paper, we propose a description of differences and similarities characterizing the above-mentioned ALS2-related rare neurodegenerative disorders, pointing attention to the effects of ALS2 mutation from molecule to organ and at the system level. Known cases were collected through a literature review and rationalized to deeply elucidate the neurodegenerative clinical outcomes as consequences of ALS2 mutations.
Keywords	amyotrophic lateral sclerosis ; brain ; genes ; humans ; juveniles ; motor neurons ; mutation ; oligomerization ; paralysis ; sclerosis ; spinal cord
Language	English
Dates of publication	2022-0105
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology11010077
Database	NAL-Catalogue (AGRICOLA)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article ; Online: Effect of Salts on the Conformational Dynamics of the Cytochrome P450 OleP.

De Sciscio, Maria Laura / Nardi, Alessandro Nicola / Parisi, Giacomo / Bulfaro, Giovanni / Costanzo, Antonella / Gugole, Elena / Exertier, Cécile / Freda, Ida / Savino, Carmelinda / Vallone, Beatrice / Montemiglio, Linda Celeste / D'Abramo, Marco

Molecules (Basel, Switzerland)

2023 Volume 28, Issue 2

Abstract: Cytochrome P450 OleP catalytic activity is strongly influenced by its structural dynamic conformational behavior. Here, we combine equilibrium-binding experiments with all-atom molecular dynamics simulations to clarify how different environments affect ... ...

Abstract	Cytochrome P450 OleP catalytic activity is strongly influenced by its structural dynamic conformational behavior. Here, we combine equilibrium-binding experiments with all-atom molecular dynamics simulations to clarify how different environments affect OleP conformational equilibrium between the open and the closed-catalytic competent-forms. Our data clearly show that at high-ionic strength conditions, the closed form is favored, and, very interestingly, different mechanisms, depending on the chemistry of the cations, can be used to rationalize such an effect.
MeSH term(s)	Salts ; Cytochrome P-450 Enzyme System/metabolism ; Protein Conformation ; Molecular Dynamics Simulation
Chemical Substances	Salts ; Cytochrome P-450 Enzyme System (9035-51-2)
Language	English
Publishing date	2023-01-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules28020832
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.MO 81: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Lack of orientation selectivity of the heme insertion in murine neuroglobin revealed by resonance Raman spectroscopy

Milazzo, Lisa / Exertier, Cécile / Becucci, Maurizio / Freda, Ida / Montemiglio, Linda Celeste / Savino, Carmelinda / Vallone, Beatrice / Smulevich, Giulietta

FEBS journal. 2020 Sept., v. 287, no. 18

2020

Abstract: Different murine neuroglobin variants showing structural and dynamic alterations that are associated with perturbation of ligand binding have been studied: the CD loop mutants characterized by an enhanced flexibility (Gly‐loop⁴⁰–⁴⁸ and Gly‐loop⁴⁴–⁴⁷), ... ...

Abstract	Different murine neuroglobin variants showing structural and dynamic alterations that are associated with perturbation of ligand binding have been studied: the CD loop mutants characterized by an enhanced flexibility (Gly‐loop⁴⁰–⁴⁸ and Gly‐loop⁴⁴–⁴⁷), the F106A mutant, and the double Gly‐loop⁴⁴–⁴⁷/F106A mutant. Their ferric resonance Raman spectra in solution and in crystals are almost identical. In the high‐frequency region, the identification of a double set of core size marker bands indicates the presence of two 6‐coordinate low spin species. The resonance Raman data, together with the corresponding crystal structures, indicate the presence of two neuroglobin conformers with a reversed (A conformer) or a canonical (B conformer) heme insertion orientation. With the identification of the marker bands corresponding to each conformer, the data indicate that the B conformer increases at the expense of the A form, predominantly in the Gly‐loop⁴⁴–⁴⁷/F106A double mutant, as confirmed by X‐ray crystallography. This is the first time that a reversed heme insertion has been identified by resonance Raman in a native 6‐coordinate low‐spin heme protein. This diagnostic tool could be extended to other heme proteins in order to detect heme orientational disorder, which are likely to be correlated to functionally relevant heme dynamics. DATABASE: Crystallographic structure: structural data are deposited in the Protein Data Bank under the 6RA6 PDB entry.
Keywords	Raman spectroscopy ; X-ray diffraction ; databases ; diagnostic techniques ; heme ; heme proteins ; ligands ; mice ; mutants
Language	English
Dates of publication	2020-09
Size	p. 4082-4097.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	NAL-AP-2-clean ; JOURNAL ARTICLE
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15241
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 2006/704: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Neuroglobin, clues to function and mechanism.

Exertier, Cécile / Montemiglio, Linda Celeste / Freda, Ida / Gugole, Elena / Parisi, Giacomo / Savino, Carmelinda / Vallone, Beatrice

Molecular aspects of medicine

2021 Volume 84, Page(s) 101055

Abstract: Neuroglobin is expressed in vertebrate brain and belongs to a branch of the globin family that diverged early in evolution. Sequence conservation and presence in nervous cells of several taxa suggests a relevant role in the nervous system, with tight ... ...

Abstract	Neuroglobin is expressed in vertebrate brain and belongs to a branch of the globin family that diverged early in evolution. Sequence conservation and presence in nervous cells of several taxa suggests a relevant role in the nervous system, with tight structural restraints. Twenty years after its discovery, a rich scientific literature provides convincing evidence of the involvement of neuroglobin in sustaining neuron viability in physiological and pathological conditions however, a full and conclusive picture of its specific function, or set of functions is still lacking. The difficulty of unambiguously assigning a precise mechanism and biochemical role to neuroglobin might arise from the participation to one or more cell mechanism that redundantly guarantee the functioning of the highly specialized and metabolically demanding central nervous system of vertebrates. Here we collect findings and hypotheses arising from recent biochemical, biophysical, structural, in cell and in vivo experimental work on neuroglobin, aiming at providing an overview of the most recent literature. Proteins are said to have jobs and hobbies, it is possible that, in the case of neuroglobin, evolution has selected for it more than one job, and support to cover for its occasional failings. Disentangling the mechanisms and roles of neuroglobin is thus a challenging task that might be achieved by considering data from different disciplines and experimental approaches.
MeSH term(s)	Animals ; Brain/metabolism ; Globins/chemistry ; Globins/genetics ; Humans ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Neuroglobin/metabolism ; Neurons/metabolism
Chemical Substances	Nerve Tissue Proteins ; Neuroglobin ; Globins (9004-22-2)
Language	English
Publishing date	2021-12-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2021.101055
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1189: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Structural insights into the DNA recognition mechanism by the bacterial transcription factor PdxR.

Freda, Ida / Exertier, Cécile / Barile, Anna / Chaves-Sanjuan, Antonio / Vega, Mirella Vivoli / Isupov, Michail N / Harmer, Nicholas J / Gugole, Elena / Swuec, Paolo / Bolognesi, Martino / Scipioni, Anita / Savino, Carmelinda / Di Salvo, Martino Luigi / Contestabile, Roberto / Vallone, Beatrice / Tramonti, Angela / Montemiglio, Linda Celeste

Nucleic acids research

2023 Volume 51, Issue 15, Page(s) 8237–8254

Abstract: Specificity in protein-DNA recognition arises from the synergy of several factors that stem from the structural and chemical signatures encoded within the targeted DNA molecule. Here, we deciphered the nature of the interactions driving DNA recognition ... ...

Abstract	Specificity in protein-DNA recognition arises from the synergy of several factors that stem from the structural and chemical signatures encoded within the targeted DNA molecule. Here, we deciphered the nature of the interactions driving DNA recognition and binding by the bacterial transcription factor PdxR, a member of the MocR family responsible for the regulation of pyridoxal 5'-phosphate (PLP) biosynthesis. Single particle cryo-EM performed on the PLP-PdxR bound to its target DNA enabled the isolation of three conformers of the complex, which may be considered as snapshots of the binding process. Moreover, the resolution of an apo-PdxR crystallographic structure provided a detailed description of the transition of the effector domain to the holo-PdxR form triggered by the binding of the PLP effector molecule. Binding analyses of mutated DNA sequences using both wild type and PdxR variants revealed a central role of electrostatic interactions and of the intrinsic asymmetric bending of the DNA in allosterically guiding the holo-PdxR-DNA recognition process, from the first encounter through the fully bound state. Our results detail the structure and dynamics of the PdxR-DNA complex, clarifying the mechanism governing the DNA-binding mode of the holo-PdxR and the regulation features of the MocR family of transcription factors.
MeSH term(s)	Bacteria/genetics ; Bacterial Proteins/metabolism ; DNA/metabolism ; Protein Binding ; Pyridoxal Phosphate/metabolism ; Transcription Factors/metabolism ; Bacillus clausii/genetics
Chemical Substances	Bacterial Proteins ; DNA (9007-49-2) ; Pyridoxal Phosphate (5V5IOJ8338) ; Transcription Factors
Language	English
Publishing date	2023-08-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkad552
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1067: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: ALS2-Related Motor Neuron Diseases: From Symptoms to Molecules.

Miceli, Marcello / Exertier, Cécile / Cavaglià, Marco / Gugole, Elena / Boccardo, Marta / Casaluci, Rossana Rita / Ceccarelli, Noemi / De Maio, Alessandra / Vallone, Beatrice / Deriu, Marco A

Biology

2022 Volume 11, Issue 1

Abstract	Infantile-onset Ascending Hereditary Spastic Paralysis, Juvenile Primary Lateral Sclerosis and Juvenile Amyotrophic Lateral Sclerosis are all motor neuron diseases related to mutations on the ALS2 gene, encoding for a 1657 amino acids protein named Alsin. This ~185 kDa multi-domain protein is ubiquitously expressed in various human tissues, mostly in the brain and the spinal cord. Several investigations have indicated how mutations within Alsin's structured domains may be responsible for the alteration of Alsin's native oligomerization state or Alsin's propensity to interact with protein partners. In this review paper, we propose a description of differences and similarities characterizing the above-mentioned ALS2-related rare neurodegenerative disorders, pointing attention to the effects of ALS2 mutation from molecule to organ and at the system level. Known cases were collected through a literature review and rationalized to deeply elucidate the neurodegenerative clinical outcomes as consequences of ALS2 mutations.
Language	English
Publishing date	2022-01-05
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology11010077
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Lack of orientation selectivity of the heme insertion in murine neuroglobin revealed by resonance Raman spectroscopy.

Milazzo, Lisa / Exertier, Cécile / Becucci, Maurizio / Freda, Ida / Montemiglio, Linda Celeste / Savino, Carmelinda / Vallone, Beatrice / Smulevich, Giulietta

The FEBS journal

2020 Volume 287, Issue 18, Page(s) 4082–4097

Abstract	Different murine neuroglobin variants showing structural and dynamic alterations that are associated with perturbation of ligand binding have been studied: the CD loop mutants characterized by an enhanced flexibility (Gly-loop
MeSH term(s)	Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Heme/chemistry ; Heme/metabolism ; Mice ; Neuroglobin/chemistry ; Neuroglobin/genetics ; Neuroglobin/metabolism ; Protein Binding ; Protein Conformation ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid ; Spectrum Analysis, Raman/methods
Chemical Substances	Neuroglobin ; Recombinant Proteins ; Heme (42VZT0U6YR)
Language	English
Publishing date	2020-02-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15241
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 260: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: Crystal structure and functional characterization of an oligosaccharide dehydrogenase from Pycnoporus cinnabarinus provides insights into fungal breakdown of lignocellulose

Cerutti, Gabriele / Gugole, Elena / Montemiglio, Linda Celeste / Turbé-Doan, Annick / Chena, Dehbia / Navarro, David / Lomascolo, Anne / Piumi, François / Exertier, Cécile / Freda, Ida / Vallone, Beatrice / Record, Eric / Savino, Carmelinda / Sciara, Giuliano

Biotechnology for biofuels. 2021 Dec., v. 14, no. 1

2021

Abstract: BACKGROUND: Fungal glucose dehydrogenases (GDHs) are FAD-dependent enzymes belonging to the glucose-methanol-choline oxidoreductase superfamily. These enzymes are classified in the “Auxiliary Activity” family 3 (AA3) of the Carbohydrate-Active enZymes ... ...

Abstract	BACKGROUND: Fungal glucose dehydrogenases (GDHs) are FAD-dependent enzymes belonging to the glucose-methanol-choline oxidoreductase superfamily. These enzymes are classified in the “Auxiliary Activity” family 3 (AA3) of the Carbohydrate-Active enZymes database, and more specifically in subfamily AA3_2, that also includes the closely related flavoenzymes aryl-alcohol oxidase and glucose 1-oxidase. Based on sequence similarity to known fungal GDHs, an AA3_2 enzyme active on glucose was identified in the genome of Pycnoporus cinnabarinus, a model Basidiomycete able to completely degrade lignin. RESULTS: In our work, substrate screening and functional characterization showed an unexpected preferential activity of this enzyme toward oligosaccharides containing a β(1→3) glycosidic bond, with the highest efficiency observed for the disaccharide laminaribiose. Despite its sequence similarity to GDHs, we defined a novel enzymatic activity, namely oligosaccharide dehydrogenase (ODH), for this enzyme. The crystallographic structures of ODH in the sugar-free form and in complex with glucose and laminaribiose unveiled a peculiar saccharide recognition mechanism which is not shared with previously characterized AA3 oxidoreductases and accounts for ODH preferential activity toward oligosaccharides. The sugar molecules in the active site of ODH are mainly stabilized through CH-π interactions with aromatic residues rather than through hydrogen bonds with highly conserved residues, as observed instead for the fungal glucose dehydrogenases and oxidases characterized to date. Finally, three sugar-binding sites were identified on ODH external surface, which were not previously observed and might be of importance in the physiological scenario. CONCLUSIONS: Structure–function analysis of ODH is consistent with its role as an auxiliary enzyme in lignocellulose degradation and unveils yet another enzymatic function within the AA3 family of the Carbohydrate-Active enZymes database. Our findings allow deciphering the molecular determinants of substrate binding and provide insight into the physiological role of ODH, opening new perspectives to exploit biodiversity for lignocellulose transformation into fuels and chemicals.
Keywords	Pycnoporus ; active sites ; aryl-alcohol oxidase ; biodiversity ; biofuels ; biotechnology ; crystal structure ; databases ; enzyme activity ; fungi ; genome ; glucose ; glycosidic linkages ; hydrogen ; lignin ; lignocellulose ; oligosaccharides ; sequence homology
Language	English
Dates of publication	2021-12
Size	p. 161.
Publishing place	BioMed Central
Document type	Article
ZDB-ID	2421351-2
ISSN	1754-6834
ISSN	1754-6834
DOI	10.1186/s13068-021-02003-y
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article ; Online: Mapping Hydrophobic Tunnels and Cavities in Neuroglobin with Noble Gas under Pressure.

Colloc'h, Nathalie / Carpentier, Philippe / Montemiglio, Laura C / Vallone, Beatrice / Prangé, Thierry

Biophysical journal

2017 Volume 113, Issue 10, Page(s) 2199–2206

Abstract: Internal cavities are crucial for conformational flexibility of proteins and can be mapped through noble gas diffusion and docking. Here we investigate the hydrophobic cavities and tunnel network in neuroglobin (Ngb), a hexacoordinated heme protein ... ...

Abstract	Internal cavities are crucial for conformational flexibility of proteins and can be mapped through noble gas diffusion and docking. Here we investigate the hydrophobic cavities and tunnel network in neuroglobin (Ngb), a hexacoordinated heme protein likely to be involved in neuroprotection, using crystallography under noble gas pressure, mostly at room temperature. In murine Ngb, a large internal cavity is involved in the heme sliding mechanism to achieve binding of gaseous ligands through coordination to the heme iron. In this study, we report that noble gases are hosted by two major sites within the internal cavity. We propose that these cavities could store oxygen and allow its relay in the heme proximity, which could correspond to NO location in the nitrite-reductase function of Ngb. Thanks to a recently designed pressurization cell using krypton at high pressure, a new gas binding site has been characterized that reveals an alternate pathway for gaseous ligands. A new gas binding site on the proximal side of the heme has also been characterized, using xenon pressure on a Ngb mutant (V140W) that binds CO with a similar rate and affinity to the wild-type, despite a reshaping of the internal cavity. Moreover, this study, to our knowledge, provides new insights into the determinants of the heme sliding mechanism, suggesting that the shift at the beginning of helix G precedes and drives this process.
MeSH term(s)	Globins/chemistry ; Globins/genetics ; Globins/metabolism ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Mutation ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Noble Gases ; Pressure ; Protein Conformation
Chemical Substances	Nerve Tissue Proteins ; Noble Gases ; neuroglobin ; Globins (9004-22-2)
Language	English
Publishing date	2017-11-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2017.10.014
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 235: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 2: Show issues

Order via subito

Details ▾

Article: Crystal structure and functional characterization of an oligosaccharide dehydrogenase from Pycnoporus cinnabarinus provides insights into fungal breakdown of lignocellulose.

Biotechnology for biofuels

2021 Volume 14, Issue 1, Page(s) 161

Abstract: Background: Fungal glucose dehydrogenases (GDHs) are FAD-dependent enzymes belonging to the glucose-methanol-choline oxidoreductase superfamily. These enzymes are classified in the "Auxiliary Activity" family 3 (AA3) of the Carbohydrate-Active enZymes ... ...

Abstract	Background: Fungal glucose dehydrogenases (GDHs) are FAD-dependent enzymes belonging to the glucose-methanol-choline oxidoreductase superfamily. These enzymes are classified in the "Auxiliary Activity" family 3 (AA3) of the Carbohydrate-Active enZymes database, and more specifically in subfamily AA3_2, that also includes the closely related flavoenzymes aryl-alcohol oxidase and glucose 1-oxidase. Based on sequence similarity to known fungal GDHs, an AA3_2 enzyme active on glucose was identified in the genome of Pycnoporus cinnabarinus, a model Basidiomycete able to completely degrade lignin. Results: In our work, substrate screening and functional characterization showed an unexpected preferential activity of this enzyme toward oligosaccharides containing a β(1→3) glycosidic bond, with the highest efficiency observed for the disaccharide laminaribiose. Despite its sequence similarity to GDHs, we defined a novel enzymatic activity, namely oligosaccharide dehydrogenase (ODH), for this enzyme. The crystallographic structures of ODH in the sugar-free form and in complex with glucose and laminaribiose unveiled a peculiar saccharide recognition mechanism which is not shared with previously characterized AA3 oxidoreductases and accounts for ODH preferential activity toward oligosaccharides. The sugar molecules in the active site of ODH are mainly stabilized through CH-π interactions with aromatic residues rather than through hydrogen bonds with highly conserved residues, as observed instead for the fungal glucose dehydrogenases and oxidases characterized to date. Finally, three sugar-binding sites were identified on ODH external surface, which were not previously observed and might be of importance in the physiological scenario. Conclusions: Structure-function analysis of ODH is consistent with its role as an auxiliary enzyme in lignocellulose degradation and unveils yet another enzymatic function within the AA3 family of the Carbohydrate-Active enZymes database. Our findings allow deciphering the molecular determinants of substrate binding and provide insight into the physiological role of ODH, opening new perspectives to exploit biodiversity for lignocellulose transformation into fuels and chemicals.
Language	English
Publishing date	2021-07-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2421351-2
ISSN	1754-6834
ISSN	1754-6834
DOI	10.1186/s13068-021-02003-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

To top

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito