Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ

C. Tomomori, T. Tanaka, R. Dutta, H. Park, S. K. Saha, Y. Zhu, R. Ishima, D. Liu, K. I. Tong, H. Kurokawa, H. Qian, M. Inouye, M. Ikura

研究成果: Article査読

204 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)729-734
ページ数6
ジャーナルNature Structural Biology
6
8
DOI
出版ステータスPublished - 1999
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 生化学
  • 遺伝学

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