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  1. Article: Unravelled proteins form blobs during translocation across nanopores.

    Sauciuc, Adina / Whittaker, Jacob / Tadema, Matthijs / Tych, Kasia / Guskov, Albert / Maglia, Giovanni

    bioRxiv : the preprint server for biology

    2024  

    Abstract: The electroosmotic-driven transport of unravelled proteins across nanopores is an important biological process that is now under investigation for the rapid analysis and sequencing of proteins. For this approach to work, however, it is crucial that the ... ...

    Abstract The electroosmotic-driven transport of unravelled proteins across nanopores is an important biological process that is now under investigation for the rapid analysis and sequencing of proteins. For this approach to work, however, it is crucial that the polymer is threaded in single file. Here we found that, contrary to the electrophoretic transport of charged polymers such as DNA, during polypeptide translocation blob-like structures typically form inside nanopores. Comparisons between different nanopore sizes, shapes and surface chemistries showed that under electroosmotic-dominated regimes single-file transport of polypeptides can be achieved using nanopores that simultaneously have an entry and an internal diameter that is smaller than the persistence length of the polymer, have a uniform non-sticky (
    Language English
    Publishing date 2024-01-25
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.01.23.576815
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Polarization Sensitive Photodetectors Based on Two-Dimensional WSe

    Guskov, Andrey / Lavrov, Sergey / Galiev, Rinat

    Nanomaterials (Basel, Switzerland)

    2022  Volume 12, Issue 11

    Abstract: In this work we show the possibility of imparting polarization-sensitive properties to two-dimensional films of graphene-like semiconductors, using ... ...

    Abstract In this work we show the possibility of imparting polarization-sensitive properties to two-dimensional films of graphene-like semiconductors, using WSe
    Language English
    Publishing date 2022-05-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2662255-5
    ISSN 2079-4991
    ISSN 2079-4991
    DOI 10.3390/nano12111854
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  3. Article ; Online: Cation permeability in CorA family of proteins.

    Stetsenko, Artem / Guskov, Albert

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 840

    Abstract: CorA proteins belong to 2-TM-GxN family of membrane proteins, and play a major role in ... ...

    Abstract CorA proteins belong to 2-TM-GxN family of membrane proteins, and play a major role in Mg
    MeSH term(s) Bacterial Proteins/metabolism ; Biological Transport ; Cation Transport Proteins/metabolism ; Cations/metabolism ; Copper/metabolism ; Escherichia coli/metabolism ; Magnesium/metabolism ; Methanocaldococcus/metabolism ; Nickel/metabolism ; Proteolipids ; Thermotoga maritima/metabolism ; Zinc/metabolism
    Chemical Substances Bacterial Proteins ; Cation Transport Proteins ; Cations ; Proteolipids ; proteoliposomes ; Copper (789U1901C5) ; Nickel (7OV03QG267) ; Magnesium (I38ZP9992A) ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2020-01-21
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-57869-z
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  4. Article: Custom Design of a Humidifier Chamber for

    Marin, Egor / Kovalev, Kirill / Poelman, Therese / Veenstra, Rick / Borshchevskiy, Valentin / Guskov, Albert

    Crystal growth & design

    2023  Volume 24, Issue 1, Page(s) 325–330

    Abstract: Membrane proteins are indispensable for every living organism, yet their structural organization remains underexplored. Despite the recent advancements in single-particle cryogenic electron microscopy and cryogenic electron tomography, which have ... ...

    Abstract Membrane proteins are indispensable for every living organism, yet their structural organization remains underexplored. Despite the recent advancements in single-particle cryogenic electron microscopy and cryogenic electron tomography, which have significantly increased the structural coverage of membrane proteins across various kingdoms, certain scientific methods, such as time-resolved crystallography, still mostly rely on crystallization techniques, such as lipidic cubic phase (LCP) or
    Language English
    Publishing date 2023-12-12
    Publishing country United States
    Document type Journal Article
    ISSN 1528-7483
    ISSN 1528-7483
    DOI 10.1021/acs.cgd.3c01034
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  5. Article ; Online: Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding.

    Wiedemann, C / Whittaker, J J / Pérez Carrillo, V H / Goretzki, B / Dajka, M / Tebbe, F / Harder, J-M / Krajczy, P R / Joseph, B / Hausch, F / Guskov, A / Hellmich, U A

    International journal of biological macromolecules

    2023  Volume 252, Page(s) 126366

    Abstract: Macrophage infectivity potentiator (MIP) proteins are widespread in human pathogens including Legionella pneumophila, the causative agent of Legionnaires' disease and protozoans such as Trypanosoma cruzi. All MIP proteins contain a FKBP (FK506 binding ... ...

    Abstract Macrophage infectivity potentiator (MIP) proteins are widespread in human pathogens including Legionella pneumophila, the causative agent of Legionnaires' disease and protozoans such as Trypanosoma cruzi. All MIP proteins contain a FKBP (FK506 binding protein)-like prolyl-cis/trans-isomerase domain that hence presents an attractive drug target. Some MIPs such as the Legionella pneumophila protein (LpMIP) have additional appendage domains of mostly unknown function. In full-length, homodimeric LpMIP, the N-terminal dimerization domain is linked to the FKBP-like domain via a long, free-standing stalk helix. Combining X-ray crystallography, NMR and EPR spectroscopy and SAXS, we elucidated the importance of the stalk helix for protein dynamics and inhibitor binding to the FKBP-like domain and bidirectional crosstalk between the different protein regions. The first comparison of a microbial MIP and a human FKBP in complex with the same synthetic inhibitor was made possible by high-resolution structures of LpMIP with a [4.3.1]-aza-bicyclic sulfonamide and provides a basis for designing pathogen-selective inhibitors. Through stereospecific methylation, the affinity of inhibitors to L. pneumophila and T. cruzi MIP was greatly improved. The resulting X-ray inhibitor-complex structures of LpMIP and TcMIP at 1.49 and 1.34 Å, respectively, provide a starting point for developing potent inhibitors against MIPs from multiple pathogenic microorganisms.
    MeSH term(s) Humans ; Legionella pneumophila/metabolism ; Scattering, Small Angle ; X-Ray Diffraction ; Bacterial Proteins/chemistry ; Tacrolimus Binding Proteins/chemistry ; Legionnaires' Disease ; Macrophages/metabolism
    Chemical Substances Bacterial Proteins ; Tacrolimus Binding Proteins (EC 5.2.1.-)
    Language English
    Publishing date 2023-08-24
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.126366
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    Zs.B 2374: Show issues Location:
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  6. Article ; Online: Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment.

    Arkhipova, Valentina / Guskov, Albert / Slotboom, Dirk J

    Nature communications

    2020  Volume 11, Issue 1, Page(s) 998

    Abstract: Glutamate transporters are cation-coupled secondary active membrane transporters that clear the neurotransmitter L-glutamate from the synaptic cleft. These transporters are homotrimers, with each protomer functioning independently by an elevator-type ... ...

    Abstract Glutamate transporters are cation-coupled secondary active membrane transporters that clear the neurotransmitter L-glutamate from the synaptic cleft. These transporters are homotrimers, with each protomer functioning independently by an elevator-type mechanism, in which a mobile transport domain alternates between inward- and outward-oriented states. Using single-particle cryo-EM we have determined five structures of the glutamate transporter homologue Glt
    MeSH term(s) Amino Acid Transport System X-AG/chemistry ; Amino Acid Transport System X-AG/genetics ; Amino Acid Transport System X-AG/metabolism ; Archaeal Proteins/chemistry ; Archaeal Proteins/genetics ; Archaeal Proteins/metabolism ; Aspartic Acid/metabolism ; Binding Sites ; Cryoelectron Microscopy ; Lipids/chemistry ; Models, Molecular ; Nanostructures/chemistry ; Protein Conformation ; Protein Structure, Quaternary ; Pyrococcus horikoshii/metabolism ; Single Molecule Imaging ; Symporters/chemistry ; Symporters/metabolism ; Thermococcus/genetics ; Thermococcus/metabolism
    Chemical Substances Amino Acid Transport System X-AG ; Archaeal Proteins ; Lipids ; Symporters ; Aspartic Acid (30KYC7MIAI)
    Language English
    Publishing date 2020-02-21
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-020-14834-8
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  7. Article ; Online: Cation Transporters of

    Volkova, Marina / Atamas, Anastasia / Tsarenko, Alexey / Rogachev, Andrey / Guskov, Albert

    Biomolecules

    2021  Volume 11, Issue 4

    Abstract: Candidiasis is the wide-spread fungal infection caused by numerous strains of yeast, with the prevalence ... ...

    Abstract Candidiasis is the wide-spread fungal infection caused by numerous strains of yeast, with the prevalence of
    Language English
    Publishing date 2021-04-16
    Publishing country Switzerland
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom11040584
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  8. Article ; Online: Crystal Structure of Levansucrase from the Gram-Negative Bacterium

    Xu, Wei / Ni, Dawei / Hou, Xiaodong / Pijning, Tjaard / Guskov, Albert / Rao, Yijian / Mu, Wanmeng

    Journal of agricultural and food chemistry

    2022  Volume 70, Issue 16, Page(s) 5095–5105

    Abstract: Microbial levansucrases (LSs, EC 2.4.1.10) have been widely studied for the synthesis of β-(2,6)-fructans (levan) from sucrose. LSs synthesize levan-type fructo-oligosaccharides, high-molecular-mass levan polymer or combinations of both. Here, we report ... ...

    Abstract Microbial levansucrases (LSs, EC 2.4.1.10) have been widely studied for the synthesis of β-(2,6)-fructans (levan) from sucrose. LSs synthesize levan-type fructo-oligosaccharides, high-molecular-mass levan polymer or combinations of both. Here, we report crystal structures of LS from the G
    MeSH term(s) Fructans/metabolism ; Gammaproteobacteria ; Hexosyltransferases/chemistry ; Sucrose/metabolism
    Chemical Substances Fructans ; Sucrose (57-50-1) ; Hexosyltransferases (EC 2.4.1.-) ; levansucrase (EC 2.4.1.10)
    Language English
    Publishing date 2022-04-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 241619-0
    ISSN 1520-5118 ; 0021-8561
    ISSN (online) 1520-5118
    ISSN 0021-8561
    DOI 10.1021/acs.jafc.2c01225
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1172: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  9. Article ; Online: Crystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from Thermophilic

    Pijning, Tjaard / Te Poele, Evelien M / de Leeuw, Tijn C / Guskov, Albert / Dijkhuizen, Lubbert

    Journal of agricultural and food chemistry

    2022  Volume 70, Issue 48, Page(s) 15283–15295

    Abstract: GtfC-type 4,6-α-glucanotransferase (α-GT) enzymes from Glycoside Hydrolase Family 70 (GH70) are of interest for the modification of starch into low-glycemic index food ingredients. Compared to the related GH70 GtfB-type α-GTs, found exclusively in lactic ...

    Abstract GtfC-type 4,6-α-glucanotransferase (α-GT) enzymes from Glycoside Hydrolase Family 70 (GH70) are of interest for the modification of starch into low-glycemic index food ingredients. Compared to the related GH70 GtfB-type α-GTs, found exclusively in lactic acid bacteria (LAB), GtfCs occur in non-LAB, share low sequence identity, lack circular permutation of the catalytic domain, and feature a single-segment auxiliary domain IV and auxiliary C-terminal domains. Despite these differences, the first crystal structure of a GtfC, GbGtfC-ΔC from
    MeSH term(s) Geobacillus/genetics ; Glycoside Hydrolases/genetics ; Starch
    Chemical Substances 4 alpha-glucanotransferase (EC 2.4.1.25) ; Glycoside Hydrolases (EC 3.2.1.-) ; Starch (9005-25-8)
    Language English
    Publishing date 2022-11-28
    Publishing country United States
    Document type Journal Article
    ZDB-ID 241619-0
    ISSN 1520-5118 ; 0021-8561
    ISSN (online) 1520-5118
    ISSN 0021-8561
    DOI 10.1021/acs.jafc.2c06394
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  10. Article ; Online: A subgroup of light-driven sodium pumps with an additional Schiff base counterion.

    Podoliak, E / Lamm, G H U / Marin, E / Schellbach, A V / Fedotov, D A / Stetsenko, A / Asido, M / Maliar, N / Bourenkov, G / Balandin, T / Baeken, C / Astashkin, R / Schneider, T R / Bateman, A / Wachtveitl, J / Schapiro, I / Busskamp, V / Guskov, A / Gordeliy, V /
    Alekseev, A / Kovalev, K

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 3119

    Abstract: Light-driven sodium pumps (NaRs) are unique ion-transporting microbial rhodopsins. The major group of NaRs is characterized by an NDQ motif and has two aspartic acid residues in the central region essential for sodium transport. Here we identify a ... ...

    Abstract Light-driven sodium pumps (NaRs) are unique ion-transporting microbial rhodopsins. The major group of NaRs is characterized by an NDQ motif and has two aspartic acid residues in the central region essential for sodium transport. Here we identify a subgroup of the NDQ rhodopsins bearing an additional glutamic acid residue in the close vicinity to the retinal Schiff base. We thoroughly characterize a member of this subgroup, namely the protein ErNaR from Erythrobacter sp. HL-111 and show that the additional glutamic acid results in almost complete loss of pH sensitivity for sodium-pumping activity, which is in contrast to previously studied NaRs. ErNaR is capable of transporting sodium efficiently even at acidic pH levels. X-ray crystallography and single particle cryo-electron microscopy reveal that the additional glutamic acid residue mediates the connection between the other two Schiff base counterions and strongly interacts with the aspartic acid of the characteristic NDQ motif. Hence, it reduces its pKa. Our findings shed light on a subgroup of NaRs and might serve as a basis for their rational optimization for optogenetics.
    MeSH term(s) Sodium-Potassium-Exchanging ATPase/metabolism ; Schiff Bases/chemistry ; Aspartic Acid ; Cryoelectron Microscopy ; Glutamic Acid ; Rhodopsins, Microbial/metabolism ; Sodium/metabolism ; Rhodopsin/chemistry
    Chemical Substances Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13) ; Schiff Bases ; Aspartic Acid (30KYC7MIAI) ; Glutamic Acid (3KX376GY7L) ; Rhodopsins, Microbial ; Sodium (9NEZ333N27) ; Rhodopsin (9009-81-8)
    Language English
    Publishing date 2024-04-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-47469-0
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