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The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network

Kiessling, Andreas R; Harris, Sarah A; Weimer, Kathleen M; Wells, Geoffrey; Goldman, Adrian; (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. 10.1111/mmi.14953. Green open access

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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.

Type: Article
Title: The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1111/mmi.14953
Publisher version: https://doi.org/10.1111/mmi.14953
Language: English
Additional information: © 2022 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Keywords: Bacterial Adhesin, Bacterial Outer Membrane Proteins, Burkholderia pseudomallei, Melioidosis, Protein Conformation, beta-Sheet, Type V Secretion Systems
UCL classification: UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy > Pharma and Bio Chemistry
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy
URI: https://discovery.ucl.ac.uk/id/eprint/10150570
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