Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB.
Acta Crystallogr F Struct Biol Commun
; 77(Pt 8): 246-253, 2021 Aug 01.
Article
em En
| MEDLINE
| ID: mdl-34341190
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 ß-barrel with a unique topology. At the top of the barrel, four loops connect the eight ß-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 1.71â
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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Rhodococcus equi
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
Alemanha