4CV7

Crystal structure of Rhodococcus equi VapB

Summary for 4CV7

• Entry DOI: 10.2210/pdb4cv7/pdb
• Descriptor: VIRULENCE ASSOCIATED PROTEIN VAPB, COBALT (II) ION (3 entities in total)
• Functional Keywords: virulence associated protein, eight-stranded antiparallel beta-barrel, b-barrel, greek key motif, toxin
• Biological source: RHODOCOCCUS EQUI
• Total number of polymer chains: 1
• Total formula weight: 12209.02

Authors

Geerds, C.,Niemann, H.H. (deposition date: 2014-03-24, release date: 2014-04-02, Last modification date: 2024-05-08)

Primary citation

Geerds, C.,Wohlmann, J.,Haas, A.,Niemann, H.H.
Structure of Rhodococcus Equi Virulence-Associated Protein B (Vapb) Reveals an Eight-Stranded Antiparallel [Beta]-Barrel Consisting of Two Greek-Key Motifs
Acta Crystallogr.,Sect.F, 70:866-, 2014

PubMed Abstract: Members of the virulence-associated protein (Vap) family from the pathogen Rhodococcus equi regulate virulence in an unknown manner. They do not share recognizable sequence homology with any protein of known structure. VapB and VapA are normally associated with isolates from pigs and horses, respectively. To contribute to a molecular understanding of Vap function, the crystal structure of a protease-resistant VapB fragment was determined at 1.4 Å resolution. The structure was solved by SAD phasing employing the anomalous signal of one endogenous S atom and two bound Co ions with low occupancy. VapB is an eight-stranded antiparallel β-barrel with a single helix. Structural similarity to avidins suggests a potential binding function. Unlike other eight- or ten-stranded β-barrels found in avidins, bacterial outer membrane proteins, fatty-acid-binding proteins and lysozyme inhibitors, Vaps do not have a next-neighbour arrangement but consist of two Greek-key motifs with strand order 41238567, suggesting an unusual or even unique topology.

PubMed: 25005079
DOI: 10.1107/S2053230X14009911

Experimental method

X-RAY DIFFRACTION (1.4 Å)