2JLI

Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion

2JLI の概要

• エントリーDOI: 10.2210/pdb2jli/pdb
• 関連するPDBエントリー: 2JLH 2JLJ
• 分子名称: YOP PROTEINS TRANSLOCATION PROTEIN (2 entities in total)
• 機能のキーワード: cell membrane, transmembrane, yersinia pestis, protein transport, type iii secretion system, plasmid, membrane, virulence, transport
• 由来する生物種: YERSINIA PESTIS
• 細胞内の位置: Cell membrane; Multi-pass membrane protein (Potential): P69986
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14376.50

構造登録者

Lountos, G.T.,Austin, B.P.,Nallamsetty, S.,Waugh, D.S. (登録日: 2008-09-09, 公開日: 2009-02-03, 最終更新日: 2024-05-08)

主引用文献

Lountos, G.T.,Austin, B.P.,Nallamsetty, S.,Waugh, D.S.
Atomic Resolution Structure of the Cytoplasmic Domain of Yersinia Pestis Yscu, a Regulatory Switch Involved in Type III Secretion.
Protein Sci., 18:467-, 2009

PubMed Abstract: Crystal structures of cleaved and uncleaved forms of the YscU cytoplasmic domain, an essential component of the type III secretion system (T3SS) in Yersinia pestis, have been solved by single-wavelength anomolous dispersion and refined with X-ray diffraction data extending up to atomic resolution (1.13 A). These crystallographic studies provide structural insights into the conformational changes induced upon auto-cleavage of the cytoplasmic domain of YscU. The structures indicate that the cleaved fragments remain bound to each other. The conserved NPTH sequence that contains the site of the N263-P264 peptide bond cleavage is found on a beta-turn which, upon cleavage, undergoes a major reorientation of the loop away from the catalytic N263, resulting in altered electrostatic surface features at the site of cleavage. Additionally, a significant conformational change was observed in the N-terminal linker regions of the cleaved and noncleaved forms of YscU which may correspond to the molecular switch that influences substrate specificity. The YscU structures determined here also are in good agreement with the auto-cleavage mechanism described for the flagellar homolog FlhB and E. coli EscU.

PubMed: 19165725
DOI: 10.1002/PRO.56

実験手法

X-RAY DIFFRACTION (1.13 Å)