Kiessling, AR orcid.org/0000-0001-9575-8153, Harris, SA, Weimer, KA et al. (2 more authors) (Cover date: July/August 2022) The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network. Molecular Microbiology, 118 (1-2). pp. 77-91. ISSN 0950-382X
Abstract
Gram-negative pathogens like Burkholderia pseudomallei use trimeric autotransporter adhesins such as BpaC as key molecules in their pathogenicity. Our 1.4 Å crystal structure of the membrane proximal part of the BpaC head domain shows that the domain is exclusively made of left-handed parallel β-roll repeats. This, the largest such structure solved, has two unique features. First, the core, rather than being composed of the canonical hydrophobic Ile and Val, is made up primarily of the hydrophilic Thr and Asn, with two different solvent channels. Second, comparing BpaC to all other left-handed parallel β-roll structures showed that the position of the head domain in the protein correlates with the number and type of charged residues. In BpaC, only negatively charged residues face the solvent – in stark contrast to the primarily positive surface charge of the left-handed parallel β-roll “type” protein, YadA. We propose extending the definitions of these head domains to include the BpaC-like head domain as a separate subtype, based on its unusual sequence, position and charge. We speculate that the function of left-handed parallel β-roll structures may differ depending on their position in the structure.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Keywords: | Bacterial Adhesin; Bacterial Outer Membrane Proteins; Burkholderia pseudomallei; Melioidosis; Protein Conformation, beta-Sheet; Type V Secretion Systems |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Physics and Astronomy (Leeds) > Theoretical Physics (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) |
Funding Information: | Funder Grant number BBSRC (Biotechnology & Biological Sciences Research Council) BB/T006048/1 EU - European Union 765042 |
Depositing User: | Symplectic Publications |
Date Deposited: | 16 Jun 2022 15:39 |
Last Modified: | 03 Aug 2022 00:56 |
Status: | Published |
Publisher: | Wiley |
Identification Number: | 10.1111/mmi.14953 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:188065 |