1ID0

CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN

1ID0 の概要

• エントリーDOI: 10.2210/pdb1id0/pdb
• 分子名称: PHOQ HISTIDINE KINASE, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: histidine kinase, phoq/phop, signal transduction, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : P23837
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17375.51

構造登録者

Marina, A.,Mott, C.,Auyzenberg, A.,Waldburger, C.D.,Hendrickson, W.A. (登録日: 2001-04-02, 公開日: 2001-10-17, 最終更新日: 2024-02-07)

主引用文献

Marina, A.,Mott, C.,Auyzenberg, A.,Hendrickson, W.A.,Waldburger, C.D.
Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism.
J.Biol.Chem., 276:41182-41190, 2001

PubMed Abstract: PhoQ is a transmembrane histidine kinase belonging to the family of two-component signal transducing systems common in prokaryotes and lower eukaryotes. In response to changes in environmental Mg(2+) concentration, PhoQ regulates the level of phosphorylated PhoP, its cognate transcriptional response-regulator. The PhoQ cytoplasmic region comprises two independently folding domains: the histidine-containing phosphotransfer domain and the ATP-binding kinase domain. We have determined the structure of the kinase domain of Escherichia coli PhoQ complexed with the non-hydrolyzable ATP analog adenosine 5'-(beta,gamma-imino)triphosphate and Mg(2+). Nucleotide binding appears to be accompanied by conformational changes in the loop that surrounds the ATP analog (ATP-lid) and has implications for interactions with the substrate phosphotransfer domain. The high resolution (1.6 A) structure reveals a detailed view of the nucleotide-binding site, allowing us to identify potential catalytic residues. Mutagenic analyses of these residues provide new insights into the catalytic mechanism of histidine phosphorylation in the histidine kinase family. Comparison with the active site of the related GHL ATPase family reveals differences that are proposed to account for the distinct functions of these proteins.

PubMed: 11493605
DOI: 10.1074/jbc.M106080200

実験手法

X-RAY DIFFRACTION (1.6 Å)