1BXD

NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ

1BXD の概要

• エントリーDOI: 10.2210/pdb1bxd/pdb
• 分子名称: PROTEIN (OSMOLARITY SENSOR PROTEIN (ENVZ)), PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total)
• 機能のキーワード: histidine kinase, osmosensor, his-asp phosphorelay system, signal transduction, transferase
• 由来する生物種: Escherichia coli BL21(DE3)
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P02933
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17923.89

構造登録者

Tanaka, T.,Saha, S.K.,Tomomori, C.,Ishima, R.,Liu, D.,Tong, K.I.,Park, H.,Dutta, R.,Qin, L.,Swindells, M.B.,Yamazaki, T.,Ono, A.M.,Kainosho, M.,Inouye, M.,Ikura, M. (登録日: 1998-10-02, 公開日: 1999-10-02, 最終更新日: 2023-12-27)

主引用文献

Tanaka, T.,Saha, S.K.,Tomomori, C.,Ishima, R.,Liu, D.,Tong, K.I.,Park, H.,Dutta, R.,Qin, L.,Swindells, M.B.,Yamazaki, T.,Ono, A.M.,Kainosho, M.,Inouye, M.,Ikura, M.
NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ.
Nature, 396:88-92, 1998

PubMed Abstract: Bacteria live in capricious environments, in which they must continuously sense external conditions in order to adjust their shape, motility and physiology. The histidine-aspartate phosphorelay signal-transduction system (also known as the two-component system) is important in cellular adaptation to environmental changes in both prokaryotes and lower eukaryotes. In this system, protein histidine kinases function as sensors and signal transducers. The Escherichia coli osmosensor, EnvZ, is a transmembrane protein with histidine kinase activity in its cytoplasmic region. The cytoplasmic region contains two functional domains: domain A (residues 223-289) contains the conserved histidine residue (H243), a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR, whereas domain B (residues 290-450) encloses several highly conserved regions (G1, G2, F and N boxes) and is able to phosphorylate H243. Here we present the solution structure of domain B, the catalytic core of EnvZ. This core has a novel protein kinase structure, distinct from the serine/threonine/tyrosine kinase fold, with unanticipated similarities to both heatshock protein 90 and DNA gyrase B.

PubMed: 9817206
DOI: 10.1038/23968

実験手法

SOLUTION NMR