4CV7

Crystal structure of Rhodococcus equi VapB

4CV7 の概要

• エントリーDOI: 10.2210/pdb4cv7/pdb
• 分子名称: VIRULENCE ASSOCIATED PROTEIN VAPB, COBALT (II) ION (3 entities in total)
• 機能のキーワード: virulence associated protein, eight-stranded antiparallel beta-barrel, b-barrel, greek key motif, toxin
• 由来する生物種: RHODOCOCCUS EQUI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12209.02

構造登録者

Geerds, C.,Niemann, H.H. (登録日: 2014-03-24, 公開日: 2014-04-02, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.4 Å)