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

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Kiessling , A R , Harris , S A , Weimer , K M , Wells , G & Goldman , A 2022 , ' The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network ' , Molecular Microbiology , vol. 118 , no. 1-2 , pp. 77-91 . https://doi.org/10.1111/mmi.14953

Title: The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network
Author: Kiessling, Andreas R.; Harris, Sarah A.; Weimer, Kathleen M.; Wells, Geoffrey; Goldman, Adrian
Contributor organization: University of Helsinki
Molecular and Integrative Biosciences Research Programme
Date: 2022-07
Language: eng
Number of pages: 15
Belongs to series: Molecular Microbiology
ISSN: 0950-382X
DOI: https://doi.org/10.1111/mmi.14953
URI: http://hdl.handle.net/10138/346713
Abstract: Gram-negative pathogens like Burkholderia pseudomallei use trimeric autotransporter adhesins such as BpaC as key molecules in their pathogenicity. Our 1.4 angstrom crystal structure of the membrane-proximal part of the BpaC head domain shows that the domain is exclusively made of left-handed parallel beta-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 beta-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 beta-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 beta-roll structures may differ depending on their position in the structure.
Subject: bacterial adhesin
bacterial outer membrane proteins
Burkholderia pseudomallei
melioidosis
protein conformation
Type V secretion systems
beta-sheet
TRIMERIC AUTOTRANSPORTER ADHESINS
SEQUENCE-ANALYSIS
DATABASE
SEARCH
YADA
MELIOIDOSIS
PREDICTION
SOFTWARE
RECEPTOR
BINDING
1182 Biochemistry, cell and molecular biology
11832 Microbiology and virology
Peer reviewed: Yes
Rights: cc_by
Usage restriction: openAccess
Self-archived version: publishedVersion


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