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• W3186402862 abstract "Virulence-associated proteins (Vaps) contribute to the virulence of the pathogen Rhodococcus equi, but their mode of action has remained elusive. All Vaps share a conserved core of about 105 amino acids that folds into a compact eight-stranded antiparallel β-barrel with a unique topology. At the top of the barrel, four loops connect the eight β-strands. Previous Vap structures did not show concave surfaces that might serve as a ligand-binding site. Here, the structure of VapB in a new crystal form was determined at 1.71 Å resolution. The asymmetric unit contains two molecules. In one of them, the loop regions at the top of the barrel adopt a different conformation from other Vap structures. An outward movement of the loops results in the formation of a hydrophobic cavity that might act as a ligand-binding site. This lends further support to the hypothesis that the structural similarity between Vaps and avidins suggests a potential binding function for Vaps." @default.
• W3186402862 created "2021-08-02" @default.
• W3186402862 creator A5000914626 @default.
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• W3186402862 date "2021-07-28" @default.
• W3186402862 modified "2023-10-11" @default.
• W3186402862 title "Conformational changes of loops highlight a potential binding site in <i>Rhodococcus equi</i> VapB" @default.
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• W3186402862 doi "https://doi.org/10.1107/s2053230x2100738x" @default.
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