1A0O

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY

1A0O の概要

• エントリーDOI: 10.2210/pdb1a0o/pdb
• 分子名称: CHEY, CHEA, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: bacterial chemotaxis, signal transduction, two-component system, histidine kinase, response regulator, chemotaxis
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P07363
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 114165.80

構造登録者

Chinardet, N.,Welch, M.,Mourey, L.,Birck, C.,Samama, J.P. (登録日: 1997-12-05, 公開日: 1998-12-30, 最終更新日: 2024-05-22)

主引用文献

Welch, M.,Chinardet, N.,Mourey, L.,Birck, C.,Samama, J.P.
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY.
Nat.Struct.Biol., 5:25-29, 1998

PubMed Abstract: Bacterial adaptation to the environment is accomplished through the coordinated activation of specific sensory receptors and signal processing proteins. Among the best characterized of these pathways are those which employ the two-component paradigm. In these systems, signal transmission is mediated by Mg(2+)-dependent phospho-relay reactions between histidine auto-kinases and phospho-accepting receiver domains in response-regulator proteins. Although this mechanism of activation is common to all response-regulators, detrimental cross-talk between different two-component pathways within the same cell is minimized through the use of specific recognition domains. Here, we report the crystal structure, at 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA. The structure suggests that molecular recognition, in this low affinity complex (KD = 2 microM), may also contribute to the mechanism of CheY activation.

PubMed: 9437425
DOI: 10.1038/nsb0198-25

実験手法

X-RAY DIFFRACTION (2.95 Å)