3CM3

High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1

3CM3 の概要

• エントリーDOI: 10.2210/pdb3cm3/pdb
• 関連するPDBエントリー: 2RF6 3CEO
• 分子名称: Dual specificity protein phosphatase, PHOSPHATE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• 機能のキーワード: dual-specificity phosphatase, vaccinia virus, vh1, hydrolase, late protein, protein phosphatase
• 由来する生物種: Vaccinia virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20513.69

構造登録者

Koksal, A.C.,Cingolani, G. (登録日: 2008-03-20, 公開日: 2009-02-10, 最終更新日: 2023-08-30)

主引用文献

Koksal, A.C.,Nardozzi, J.D.,Cingolani, G.
Dimeric Quaternary Structure of the Prototypical Dual Specificity Phosphatase VH1.
J.Biol.Chem., 284:10129-10137, 2009

PubMed Abstract: The Vaccinia virus H1 gene product, VH1, is a dual specificity phosphatase that down-regulates the cellular antiviral response by dephosphorylating STAT1. The crystal structure of VH1, determined at 1.32 A resolution, reveals a novel dimeric quaternary structure, which exposes two active sites spaced approximately 39 A away from each other. VH1 forms a stable dimer via an extensive domain swap of the N-terminal helix (residues 1-20). In vitro, VH1 can dephosphorylate activated STAT1, in a reaction that is competed by the nuclear transport adapter importin alpha5. Interestingly, VH1 is inactive with respect to STAT1 bound to DNA, suggesting that the viral phosphatase acts predominantly on the cytoplasmic pool of activated STAT1. We propose that the dimeric quaternary structure of VH1 is essential for specific recognition of activated STAT1, which prevents its nuclear translocation, thus blocking interferon-gamma signal transduction and antiviral response.

PubMed: 19211553
DOI: 10.1074/jbc.M808362200

実験手法

X-RAY DIFFRACTION (1.32 Å)