7b1z

Virulence-associated protein VapB from the intracellular pathogen Rhodococcus equi

spinqualitylabelsall models 7b1z, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7b1z is a 2 chain structure with sequence from Rhodococcus equi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.71Å Ligands: GOL, NO3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B4F366_RHOHA Publication Abstract from PubMed 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. Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB.,Geerds C, Haas A, Niemann HH Acta Crystallogr F Struct Biol Commun. 2021 Aug 1;77(Pt 8):246-253. doi: , 10.1107/S2053230X2100738X. Epub 2021 Jul 28. PMID:34341190 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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