1JBE

1.08 A Structure of apo-Chey reveals meta-active conformation

1JBE の概要

• エントリーDOI: 10.2210/pdb1jbe/pdb
• 関連するPDBエントリー: 3CHY
• 分子名称: Chemotaxis protein CheY, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: chey, chemotaxis, signaling protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14434.51

構造登録者

Simonovic, M.,Volz, K. (登録日: 2001-06-04, 公開日: 2001-08-08, 最終更新日: 2024-11-20)

主引用文献

Simonovic, M.,Volz, K.
A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY.
J.Biol.Chem., 276:28637-28640, 2001

PubMed Abstract: CheY is the best characterized member of the response regulator superfamily, and as such it has become the principal model for understanding the initial molecular mechanisms of signaling in two-component systems. Normal signaling by response regulators requires phosphorylation, in combination with an activation mechanism whose conformational effects are not completely understood. CheY activation involves three events, phosphorylation, a conformational change in the beta(4)--alpha(4) loop, and a rotational restriction of the side chain of tyrosine 106. An outstanding question concerns the nature of an active conformation in the apoCheY population. The details of this 1.08-A resolution crystal structure of wild-type apoCheY shows the beta(4)--alpha(4) loop in two distinctly different conformations that sterically correlate with the two rotameric positions of the tyrosine 106 side chain. One of these conformational states of CheY is the inactive form, and we propose that the other is a meta-active form, responsible for the active properties seen in apoCheY.

PubMed: 11410584
DOI: 10.1074/jbc.C100295200

実験手法

X-RAY DIFFRACTION (1.08 Å)