1bxd

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

Overview

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.

About this Structure

1BXD is a Single protein structure of sequence from Escherichia coli with ANP as ligand. Full crystallographic information is available from OCA.

Reference

NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ., Tanaka T, Saha SK, Tomomori C, Ishima R, Liu D, Tong KI, Park H, Dutta R, Qin L, Swindells MB, Yamazaki T, Ono AM, Kainosho M, Inouye M, Ikura M, Nature. 1998 Nov 5;396(6706):88-92. PMID:9817206

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