1JOY

SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR.

1JOY の概要

• エントリーDOI: 10.2210/pdb1joy/pdb
• 分子名称: PROTEIN (ENVZ_ECOLI) (1 entity in total)
• 機能のキーワード: histidine kinase, sensory transduction, osmolarity sensor protein, inner membrane, phosphorylation, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P02933
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15187.34

構造登録者

Tomomori, C.,Tanaka, T.,Dutta, R.,Park, H.,Saha, S.K.,Zhu, Y.,Ishima, R.,Liu, D.,Tong, K.I.,Kurokawa, H.,Qian, H.,Inouye, M.,Ikura, M. (登録日: 1998-12-28, 公開日: 2000-01-12, 最終更新日: 2023-12-27)

主引用文献

Tomomori, C.,Tanaka, T.,Dutta, R.,Park, H.,Saha, S.K.,Zhu, Y.,Ishima, R.,Liu, D.,Tong, K.I.,Kurokawa, H.,Qian, H.,Inouye, M.,Ikura, M.
Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ.
Nat.Struct.Biol., 6:729-734, 1999

PubMed Abstract: Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.

PubMed: 10426948
DOI: 10.1038/11495

実験手法

SOLUTION NMR