1R6F

The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague

1R6F の概要

• エントリーDOI: 10.2210/pdb1r6f/pdb
• 分子名称: Virulence-associated V antigen (1 entity in total)
• 機能のキーワード: coiled-coil, protein binding
• 由来する生物種: Yersinia pestis
• 細胞内の位置: Secreted: P21206
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35158.56

構造登録者

Derewenda, U.,Mateja, A.,Devedjiev, Y.,Routzahn, K.M.,Evdokimov, A.G.,Derewenda, Z.S.,Waugh, D.S. (登録日: 2003-10-15, 公開日: 2004-03-09, 最終更新日: 2024-02-14)

主引用文献

Derewenda, U.,Mateja, A.,Devedjiev, Y.,Routzahn, K.M.,Evdokimov, A.G.,Derewenda, Z.S.,Waugh, D.S.
The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
Structure, 12:301-306, 2004

PubMed Abstract: The LcrV protein (V-antigen) is a multifunctional virulence factor in Yersinia pestis, the causative agent of plague. LcrV regulates the translocation of cytotoxic effector proteins from the bacterium into the cytosol of mammalian cells via a type III secretion system, possesses antihost activities of its own, and is also an active and passive mediator of resistance to disease. Although a crystal structure of this protein has been actively sought for better understanding of its role in pathogenesis, the wild-type LcrV was found to be recalcitrant to crystallization. We employed a surface entropy reduction mutagenesis strategy to obtain crystals of LcrV that diffract to 2.2 A and determined its structure. The refined model reveals a dumbbell-like molecule with a novel fold that includes an unexpected coiled-coil motif, and provides a detailed three-dimensional roadmap for exploring structure-function relationships in this essential virulence determinant.

PubMed: 14962390
DOI: 10.1016/j.str.2004.03.008

実験手法

X-RAY DIFFRACTION (2.17 Å)