7B1Z
Virulence-associated protein VapB from the intracellular pathogen Rhodococcus equi
Summary for 7B1Z
| Entry DOI | 10.2210/pdb7b1z/pdb |
| Related | 4CV7 |
| Descriptor | Virulence associated protein VapB, GLYCEROL, NITRATE ION, ... (4 entities in total) |
| Functional Keywords | beta barrel, conformational change, ligand binding site, virulence factor, toxin |
| Biological source | Rhodococcus hoagii |
| Total number of polymer chains | 2 |
| Total formula weight | 24766.80 |
| Authors | Geerds, C.,Niemann, H.H. (deposition date: 2020-11-25, release date: 2021-07-28, Last modification date: 2024-01-31) |
| Primary citation | Geerds, C.,Haas, A.,Niemann, H.H. Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB. Acta Crystallogr.,Sect.F, 77:246-253, 2021 Cited by PubMed 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. PubMed: 34341190DOI: 10.1107/S2053230X2100738X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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