1HUF

CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TYROSINE PHOSPHATASE YOPH FROM YERSINIA PESTIS.

1HUF の概要

• エントリーDOI: 10.2210/pdb1huf/pdb
• 関連するPDBエントリー: 1YPT
• 分子名称: TYROSINE PHOSPHATASE YOPH (2 entities in total)
• 機能のキーワード: helical bundle, beta hairpin, hydrolase
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15080.78

構造登録者

Evdokimov, A.G.,Waugh, D.S. (登録日: 2001-01-04, 公開日: 2001-05-23, 最終更新日: 2024-02-07)

主引用文献

Evdokimov, A.G.,Tropea, J.E.,Routzahn, K.M.,Copeland, T.D.,Waugh, D.S.
Structure of the N-terminal domain of Yersinia pestis YopH at 2.0 A resolution.
Acta Crystallogr.,Sect.D, 57:793-799, 2001

PubMed Abstract: Yersinia pestis, the causative agent of bubonic plague, injects effector proteins into the cytosol of mammalian cells that enable the bacterium to evade the immune response of the infected organism by interfering with eukaryotic signal transduction pathways. YopH is a modular effector composed of a C-terminal protein tyrosine phosphatase (PTPase) domain and a multifunctional N-terminal domain that not only orchestrates the secretion and translocation of YopH into eukaryotic cells but also binds tyrosine-phosphorylated target proteins to mediate substrate recognition. The crystal structure of the N-terminal domain of YopH (YopH(N); residues 1-130) has been determined at 2.0 A resolution. The amino-acid sequences that target YopH for secretion from the bacterium and translocation into eukaryotic cells form integral parts of this compactly folded domain. The structure of YopH(N) bears no resemblance to eukaryotic phosphotyrosine-binding domains, nor is it reminiscent of any known fold. Residues that have been implicated in phosphotyrosine-dependent protein binding are clustered together on one face of YopH(N), but the structure does not suggest a mechanism for protein-phosphotyrosine recognition.

PubMed: 11375498
DOI: 10.1107/S0907444901004875

実験手法

X-RAY DIFFRACTION (2 Å)