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- TitleConformational changes of loops highlight a potential binding site in Rhodococcus equi VapB
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- Is part ofActa crystallographica. Section F: Structural biology communications, Vol. 77 Issue Pt 8
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- LanguageEnglish
- Document typeJournal Article
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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 beta-barrel with a unique topology. At the top of the barrel, four loops connect the eight beta-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 A 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. open access.
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