2CHY

THREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS

2CHY の概要

• エントリーDOI: 10.2210/pdb2chy/pdb
• 分子名称: CHEY (1 entity 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: 14025.25

構造登録者

Mottonen, J.M.,Stock, A.M.,Stock, J.B.,Schutt, C.E. (登録日: 1990-05-17, 公開日: 1990-07-15, 最終更新日: 2024-02-14)

主引用文献

Stock, A.M.,Mottonen, J.M.,Stock, J.B.,Schutt, C.E.
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis.
Nature, 337:745-749, 1989

PubMed Abstract: Homologies among bacterial signal transduction proteins suggest that a common mechanism mediates processes such as chemotaxis, osmoregulation, sporulation, virulence, and responses to nitrogen, phosphorous and oxygen deprivation. A common kinase-mediated phosphotransfer reaction has recently been identified in chemotaxis, nitrogen regulation, and osmoregulation. In chemotaxis, the CheA kinase passes a phosphoryl group to the cytoplasmic protein CheY, which functions as a phosphorylation-activated switch that interacts with flagellar components to regulate motility. We report here the X-ray crystal structure of the Salmonella typhimurium CheY protein. The determination of the structure was facilitated by the use of site-specific mutagenesis to engineer heavy-atom binding sites. CheY is a single-domain protein composed of a doubly wound five-stranded parallel beta-sheet. The phosphoacceptor site in CheY is probably a cluster of aspartic-acid side chains near the C-terminal edge of the beta-sheet. The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site.

PubMed: 2645526
DOI: 10.1038/337745a0

実験手法

X-RAY DIFFRACTION (2.7 Å)