1joy | pdb_00001joy
SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR.
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Overview
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.
About this Structure
1JOY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ., Tomomori C, Tanaka T, Dutta R, Park H, Saha SK, Zhu Y, Ishima R, Liu D, Tong KI, Kurokawa H, Qian H, Inouye M, Ikura M, Nat Struct Biol. 1999 Aug;6(8):729-34. PMID:10426948
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