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  1. Article ; Online: Crystallographic and biochemical analyses of a far-red allophycocyanin to address the mechanism of the super-red-shift.

    Zhou, Li-Juan / Höppner, Astrid / Wang, Yi-Qing / Hou, Jian-Yun / Scheer, Hugo / Zhao, Kai-Hong

    Photosynthesis research

    2024  

    Abstract: Far-red absorbing allophycocyanins (APC), identified in cyanobacteria capable of FRL photoacclimation (FaRLiP) and low-light photoacclimation (LoLiP), absorb far-red light, functioning in energy transfer as light-harvesting proteins. We report an ... ...

    Abstract Far-red absorbing allophycocyanins (APC), identified in cyanobacteria capable of FRL photoacclimation (FaRLiP) and low-light photoacclimation (LoLiP), absorb far-red light, functioning in energy transfer as light-harvesting proteins. We report an optimized method to obtain high purity far-red absorbing allophycocyanin B, AP-B2, of Chroococcidiopsis thermalis sp. PCC7203 by synthesis in Escherichia coli and an improved purification protocol. The crystal structure of the trimer, (PCB-ApcD5/PCB-ApcB2)
    Language English
    Publishing date 2024-01-06
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1475688-2
    ISSN 1573-5079 ; 0166-8595
    ISSN (online) 1573-5079
    ISSN 0166-8595
    DOI 10.1007/s11120-023-01066-2
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  2. Article: The structure of MadC from

    Knospe, C Vivien / Kamel, Michael / Spitz, Olivia / Hoeppner, Astrid / Galle, Stefanie / Reiners, Jens / Kedrov, Alexej / Smits, Sander H J / Schmitt, Lutz

    Frontiers in microbiology

    2023  Volume 13, Page(s) 1057217

    Abstract: The rapid emergence of microbial multi-resistance against antibiotics has led to intense search for alternatives. One of these alternatives are ribosomally synthesized and post-translationally modified peptides (RiPPs), especially lantibiotics. They are ... ...

    Abstract The rapid emergence of microbial multi-resistance against antibiotics has led to intense search for alternatives. One of these alternatives are ribosomally synthesized and post-translationally modified peptides (RiPPs), especially lantibiotics. They are active in a low nanomolar range and their high stability is due to the presence of characteristic (methyl-) lanthionine rings, which makes them promising candidates as bacteriocides. However, innate resistance against lantibiotics exists in nature, emphasizing the need for artificial or tailor-made lantibiotics. Obviously, such an approach requires an in-depth mechanistic understanding of the modification enzymes, which catalyze the formation of (methyl-)lanthionine rings. Here, we determined the structure of a class I cyclase (MadC), involved in the modification of maddinglicin (MadA)
    Language English
    Publishing date 2023-01-18
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2022.1057217
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  3. Article ; Online: Crystal structure of the sugar acid-binding protein CxaP from a TRAP transporter in Advenella mimigardefordensis strain DPN7

    Schäfer, Lukas / Meinert-Berning, Christina / Kobus, Stefanie / Höppner, Astrid / Smits, Sander H J / Steinbüchel, Alexander

    The FEBS journal

    2021  Volume 288, Issue 16, Page(s) 4905–4917

    Abstract: Recently, CxaP, a sugar acid substrate binding protein (SBP) from Advenella mimigardefordensis strain ... ...

    Abstract Recently, CxaP, a sugar acid substrate binding protein (SBP) from Advenella mimigardefordensis strain DPN7
    MeSH term(s) Alcaligenaceae/chemistry ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Crystallography, X-Ray ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/metabolism ; Models, Molecular ; Sugar Acids/chemistry ; Sugar Acids/metabolism
    Chemical Substances Bacterial Proteins ; Membrane Transport Proteins ; Sugar Acids
    Language English
    Publishing date 2021-03-11
    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.15789
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    Zs.A 260: Show issues Location:
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  4. Article: Crystal structure of the sugar acid‐binding protein CxaP from a TRAP transporter in Advenella mimigardefordensis strain DPN7T

    Schäfer, Lukas / Meinert‐Berning, Christina / Kobus, Stefanie / Höppner, Astrid / Smits, Sander H. J. / Steinbüchel, Alexander

    FEBS journal. 2021 Aug., v. 288, no. 16

    2021  

    Abstract: Recently, CxaP, a sugar acid substrate binding protein (SBP) from Advenella mimigardefordensis strain DPN7ᵀ, was identified as part of a novel sugar uptake strategy. In the present study, the protein was successfully crystallized. Although several SBP ... ...

    Abstract Recently, CxaP, a sugar acid substrate binding protein (SBP) from Advenella mimigardefordensis strain DPN7ᵀ, was identified as part of a novel sugar uptake strategy. In the present study, the protein was successfully crystallized. Although several SBP structures of tripartite ATP‐independent periplasmic transporters have already been solved, this is the first structure of an SBP accepting multiple sugar acid ligands. Protein crystals were obtained with bound d‐xylonic acid, d‐fuconic acid d‐galactonic and d‐gluconic acid, respectively. The protein shows the typical structure of an SBP of a tripartite ATP‐independent periplasmic transporter consisting of two domains linked by a hinge and spanned by a long α‐helix. By analysis of the structure, the substrate binding site of the protein was identified. The carboxylic group of the sugar acids interacts with Arg175, whereas the coordination of the hydroxylic groups at positions C2 and C3 is most probably realized by Arg154 and Asn151. Furthermore, it was observed that 2‐keto‐3‐deoxy‐d‐gluconic acid is bound in protein crystals that were crystallized without the addition of any ligand, indicating that this molecule is prebound to the protein and is displaced by the other ligands if they are available. DATABASE: Structural data of CxaP complexes are available in the worldwide Protein Data Bank (https://www.rcsb.org) under the accession codes 7BBR (2‐keto‐3‐deoxy‐d‐gluconic acid), 7BCR (d‐galactonic acid), 7BCN (d‐xylonic acid), 7BCO (d‐fuconic acid) and 7BCP (d‐gluconic acid).
    Keywords acids ; binding sites ; crystal proteins ; crystal structure ; crystallization ; journals ; ligands ; protein binding ; strains ; sugar acids ; sugar crystals ; transporters
    Language English
    Dates of publication 2021-08
    Size p. 4905-4917.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.15789
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  5. Article ; Online: DNA-binding and protein structure of nuclear factors likely acting in genetic information processing in the

    Macorano, Luis / Binny, Taniya M / Spiegl, Tobias / Klimenko, Victoria / Singer, Anna / Oberleitner, Linda / Applegate, Violetta / Seyffert, Sarah / Stefanski, Anja / Gremer, Lothar / Gertzen, Christoph G W / Höppner, Astrid / Smits, Sander H J / Nowack, Eva C M

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 27, Page(s) e2221595120

    Abstract: The chromatophores ... ...

    Abstract The chromatophores in
    MeSH term(s) Biological Evolution ; Photosynthesis/genetics ; Rhizaria ; Chromatophores/metabolism ; Anti-Infective Agents/metabolism
    Chemical Substances Anti-Infective Agents
    Language English
    Publishing date 2023-06-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2221595120
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
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  6. Article ; Online: Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism.

    Minges, Alexander / Höppner, Astrid / Groth, Georg

    Protein science : a publication of the Protein Society

    2017  Volume 26, Issue 8, Page(s) 1667–1673

    Abstract: Pyruvate phosphate dikinase (PPDK) is an essential enzyme of both the ... ...

    Abstract Pyruvate phosphate dikinase (PPDK) is an essential enzyme of both the C
    MeSH term(s) Biocatalysis ; Catalytic Domain ; Cloning, Molecular ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Flaveria/chemistry ; Flaveria/enzymology ; Gene Expression ; Models, Molecular ; Phosphoenolpyruvate/chemistry ; Phosphoenolpyruvate/metabolism ; Plant Proteins/chemistry ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Domains ; Pyruvate, Orthophosphate Dikinase/chemistry ; Pyruvate, Orthophosphate Dikinase/genetics ; Pyruvate, Orthophosphate Dikinase/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Substrate Specificity ; Thermodynamics
    Chemical Substances Plant Proteins ; Recombinant Proteins ; Phosphoenolpyruvate (73-89-2) ; Pyruvate, Orthophosphate Dikinase (EC 2.7.9.1)
    Language English
    Publishing date 2017-05-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.3184
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    Zs.A 3407: Show issues Location:
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    Zs.MO 1: Show issues

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  7. Book ; Online ; Thesis: Enzym-Substratkomplexe der Quinat-Dehydrogenase aus Corynebacterium glutamicum

    Höppner, Astrid

    Strukturen, Katalyse und Spezifitäten

    2008  

    Author's details vorgelegt von Astrid Höppner
    Language German
    Size Online-Ressource (PDF-Datei: 147 S., 45,4 MB)
    Publisher Univ.-Bibliothek
    Publishing place Köln
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss.--Köln, 2008
    Database Former special subject collection: coastal and deep sea fishing

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  8. Book ; Online ; Thesis: Enzym-Substratkomplexe der Quinat-Dehydrogenase aus Corynebacterium glutamicum

    Höppner, Astrid

    Strukturen, Katalyse und Spezifitäten

    2008  

    Author's details vorgelegt von Astrid Höppner
    Language German
    Size Online-Ressource (PDF-Datei: 147 S., 45,4 MB)
    Publisher Univ.-Bibliothek
    Publishing place Köln
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss.--Köln, 2008
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  9. Article ; Online: Crystal structures of a novel family IV esterase in free and substrate-bound form.

    Höppner, Astrid / Bollinger, Alexander / Kobus, Stefanie / Thies, Stephan / Coscolín, Cristina / Ferrer, Manuel / Jaeger, Karl-Erich / Smits, Sander H J

    The FEBS journal

    2021  Volume 288, Issue 11, Page(s) 3570–3584

    Abstract: Bacterial lipolytic enzymes of family IV are homologs of the mammalian hormone-sensitive lipases (HSL) and have been successfully used for various biotechnological applications. The broad substrate specificity and ability for enantio-, regio-, and ... ...

    Abstract Bacterial lipolytic enzymes of family IV are homologs of the mammalian hormone-sensitive lipases (HSL) and have been successfully used for various biotechnological applications. The broad substrate specificity and ability for enantio-, regio-, and stereoselective hydrolysis are remarkable features of enzymes from this class. Many crystal structures are available for esterases and lipases, but structures of enzyme-substrate or enzyme-inhibitor complexes are less frequent although important to understand the molecular basis of enzyme-substrate interaction and to rationalize biochemical enzyme characteristics. Here, we report on the structures of a novel family IV esterase isolated from a metagenomic screen, which shows a broad substrate specificity. We solved the crystal structures in the apo form and with a bound substrate analogue at 1.35 and 1.81 Å resolution, respectively. This enzyme named PtEst1 hydrolyzed more than 60 out 96 structurally different ester substrates thus being substrate promiscuous. Its broad substrate specificity is in accord with a large active site cavity, which is covered by an α-helical cap domain. The substrate analogue methyl 4-methylumbelliferyl hexylphosphonate was rapidly hydrolyzed by the enzyme leading to a complete inactivation caused by covalent binding of phosphinic acid to the catalytic serine. Interestingly, the alcohol leaving group 4-methylumbelliferone was found remaining in the active site cavity, and additionally, a complete inhibitor molecule was found at the cap domain next to the entrance of the substrate tunnel. This unique situation allowed gaining valuable insights into the role of the cap domain for enzyme-substrate interaction of esterases belonging to family IV. DATABASE: Structural data of PtEst1 are available in the worldwide protein data bank (https://www.rcsb.org) under the accession codes: 6Z68 (apo-PtEst1) and 6Z69 (PtEst1-inhibitor complex).
    MeSH term(s) Crystallography, X-Ray ; Esterases/ultrastructure ; Lipase/ultrastructure ; Metagenome/genetics ; Protein Conformation ; Pseudonocardia/chemistry ; Pseudonocardia/genetics ; Pseudonocardia/ultrastructure ; Substrate Specificity/genetics
    Chemical Substances Esterases (EC 3.1.-) ; Lipase (EC 3.1.1.3)
    Language English
    Publishing date 2021-01-06
    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.15680
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  10. Article: Crystal structures of a novel family IV esterase in free and substrate‐bound form

    Höppner, Astrid / Bollinger, Alexander / Kobus, Stefanie / Thies, Stephan / Coscolín, Cristina / Ferrer, Manuel / Jaeger, Karl‐Erich / Smits, Sander H. J

    FEBS journal. 2021 June, v. 288, no. 11

    2021  

    Abstract: Bacterial lipolytic enzymes of family IV are homologs of the mammalian hormone‐sensitive lipases (HSL) and have been successfully used for various biotechnological applications. The broad substrate specificity and ability for enantio‐, regio‐, and ... ...

    Abstract Bacterial lipolytic enzymes of family IV are homologs of the mammalian hormone‐sensitive lipases (HSL) and have been successfully used for various biotechnological applications. The broad substrate specificity and ability for enantio‐, regio‐, and stereoselective hydrolysis are remarkable features of enzymes from this class. Many crystal structures are available for esterases and lipases, but structures of enzyme–substrate or enzyme–inhibitor complexes are less frequent although important to understand the molecular basis of enzyme–substrate interaction and to rationalize biochemical enzyme characteristics. Here, we report on the structures of a novel family IV esterase isolated from a metagenomic screen, which shows a broad substrate specificity. We solved the crystal structures in the apo form and with a bound substrate analogue at 1.35 and 1.81 Å resolution, respectively. This enzyme named PtEst1 hydrolyzed more than 60 out 96 structurally different ester substrates thus being substrate promiscuous. Its broad substrate specificity is in accord with a large active site cavity, which is covered by an α‐helical cap domain. The substrate analogue methyl 4‐methylumbelliferyl hexylphosphonate was rapidly hydrolyzed by the enzyme leading to a complete inactivation caused by covalent binding of phosphinic acid to the catalytic serine. Interestingly, the alcohol leaving group 4‐methylumbelliferone was found remaining in the active site cavity, and additionally, a complete inhibitor molecule was found at the cap domain next to the entrance of the substrate tunnel. This unique situation allowed gaining valuable insights into the role of the cap domain for enzyme–substrate interaction of esterases belonging to family IV. DATABASE: Structural data of PtEst1 are available in the worldwide protein data bank (https://www.rcsb.org) under the accession codes: 6Z68 (apo‐PtEst1) and 6Z69 (PtEst1‐inhibitor complex).
    Keywords active sites ; alcohols ; carboxylic ester hydrolases ; enzyme substrates ; hydrolysis ; mammals ; metagenomics ; serine ; stereoselectivity ; substrate specificity
    Language English
    Dates of publication 2021-06
    Size p. 3570-3584.
    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.15680
    Database NAL-Catalogue (AGRICOLA)

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