1joy

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1joy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1joy OCA], [http://www.ebi.ac.uk/pdbsum/1joy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1joy RCSB]</span>
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[[Category: sensory transduction]]
[[Category: sensory transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:36:49 2008''

Revision as of 18:36, 30 March 2008


PDB ID 1joy

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR.


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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