1XKO

Structure of Thermotoga maritima CheX

1XKO の概要

• エントリーDOI: 10.2210/pdb1xko/pdb
• 関連するPDBエントリー: 1SQU
• 分子名称: CHEMOTAXIS protein cheX (2 entities in total)
• 機能のキーワード: chemotaxis, signal transduction, protein phosphatase, attractant
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33761.11

構造登録者

Park, S.Y.,Chao, X.,Gonzalez-Bonet, G.,Beel, B.D.,Bilwes, A.M.,Crane, B.R. (登録日: 2004-09-29, 公開日: 2004-12-07, 最終更新日: 2023-08-23)

主引用文献

Park, S.Y.,Chao, X.,Gonzalez-Bonet, G.,Beel, B.D.,Bilwes, A.M.,Crane, B.R.
Structure and Function of an Unusual Family of Protein Phosphatases; The Bacterial Chemotaxis Proteins CheC and CheX.
Mol.Cell, 16:563-574, 2004

PubMed Abstract: In bacterial chemotaxis, phosphorylated CheY levels control the sense of flagella rotation and thereby determine swimming behavior. In E. coli, CheY dephosphorylation by CheZ extinguishes the switching signal. But, instead of CheZ, many chemotactic bacteria contain CheC, CheD, and/or CheX. The crystal structures of T. maritima CheC and CheX reveal a common fold unlike that of any other known protein. Unlike CheC, CheX dimerizes via a continuous beta sheet between subunits. T. maritima CheC, as well as CheX, dephosphorylate CheY, although CheC requires binding of CheD to achieve the activity of CheX. Structural analyses identified one conserved active site in CheX and two in CheC; mutations therein reduce CheY-phosphatase activity, but only mutants of two invariant asparagine residues are completely inactive even in the presence of CheD. Our structures indicate that the flagellar switch components FliY and FliM resemble CheC more closely than CheX, but attribute phosphatase activity only to FliY.

PubMed: 15546616
DOI: 10.1016/j.molcel.2004.10.018

実験手法

X-RAY DIFFRACTION (2.48 Å)