7B1Z

Virulence-associated protein VapB from the intracellular pathogen Rhodococcus equi

7B1Z の概要

• エントリーDOI: 10.2210/pdb7b1z/pdb
• 関連するPDBエントリー: 4CV7
• 分子名称: Virulence associated protein VapB, GLYCEROL, NITRATE ION, ... (4 entities in total)
• 機能のキーワード: beta barrel, conformational change, ligand binding site, virulence factor, toxin
• 由来する生物種: Rhodococcus hoagii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24766.80

構造登録者

Geerds, C.,Niemann, H.H. (登録日: 2020-11-25, 公開日: 2021-07-28, 最終更新日: 2024-01-31)

主引用文献

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

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: 34341190
DOI: 10.1107/S2053230X2100738X

実験手法

X-RAY DIFFRACTION (1.71 Å)