1EAY

CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI

1EAY の概要

• エントリーDOI: 10.2210/pdb1eay/pdb
• 分子名称: CHEY, CHEA (3 entities in total)
• 機能のキーワード: signal transduction complex, kinase, response regulator, chemotaxis
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P06143 P07363
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 43998.44

構造登録者

Mcevoy, M.M.,Hausrath, A.C.,Randolph, G.B.,Remington, S.J.,Dahlquist, F.W. (登録日: 1998-04-23, 公開日: 1998-07-15, 最終更新日: 2024-05-22)

主引用文献

McEvoy, M.M.,Hausrath, A.C.,Randolph, G.B.,Remington, S.J.,Dahlquist, F.W.
Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway.
Proc.Natl.Acad.Sci.USA, 95:7333-7338, 1998

PubMed Abstract: The crystal structure at 2.0-A resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain (P2) of the kinase CheA is presented. The binding interface involves the fourth and fifth helices and fifth beta-strand of CheY and both helices of P2. Surprisingly, the two heterodimers in the asymmetric unit have two different binding modes involving the same interface, suggesting some flexibility in the binding regions. Significant conformational changes have occurred in CheY compared with previously determined unbound structures. The active site of CheY is exposed by the binding of the kinase domain, possibly to enhance phosphotransfer from CheA to CheY. The conformational changes upon complex formation as well as the observation that there are two different binding modes suggest that the plasticity of CheY is an essential feature of response regulator function.

PubMed: 9636149
DOI: 10.1073/pnas.95.13.7333

実験手法

X-RAY DIFFRACTION (2 Å)