1bxd

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

spinqualitylabelsall models 1bxd, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bxd is a 1 chain structure with sequence from Escherichia coli bl21(de3). Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP Resources: FirstGlance, OCA, RCSB, PDBsum Function [ENVZ_ECOLI] Member of the two-component regulatory system EnvZ/OmpR involved in the regulation of osmoregulation (genes ompF and ompC). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA