2CHF

STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND THE MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS

2CHF の概要

• エントリーDOI: 10.2210/pdb2chf/pdb
• 分子名称: CHEY (2 entities in total)
• 機能のキーワード: signal transduction protein
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cytoplasm: P0A2D5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14009.19

構造登録者

Stock, A.,Martinez-Hackert, E.,Rasmussen, B.,West, A.,Stock, J.,Ringe, D.,Petsko, G. (登録日: 1994-01-17, 公開日: 1994-04-30, 最終更新日: 2024-02-14)

主引用文献

Stock, A.M.,Martinez-Hackert, E.,Rasmussen, B.F.,West, A.H.,Stock, J.B.,Ringe, D.,Petsko, G.A.
Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis.
Biochemistry, 32:13375-13380, 1993

PubMed Abstract: The response regulator protein of bacterial chemotaxis, CheY, is representative of a large family of signal transduction proteins that function as phosphorylation-activated switches to regulate the activities of associated effector domains. These regulators catalyze the metal ion-dependent phosphoryl transfer and dephosphorylation reactions that control the effector activities. The crystal structures of Salmonella typhimurium CheY with and without Mg2+ bound at the active site have been determined and refined at 1.8-A resolution. While the overall structures of metal-bound and metal-free CheY are similar, significant rearrangements occur within the active site involving the three most highly conserved residues of the response regulator family. Conservation of the cluster of carboxylate side chains at the active site of response regulator domains can be rationalized in terms of their role in coordinating the catalytically essential divalent metal ion. The Mg2+ coordination geometry provides insights to the mechanism of phosphoryl transfer.

PubMed: 8257674
DOI: 10.1021/bi00212a001

実験手法

X-RAY DIFFRACTION (1.8 Å)