1JOY: SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR

Citation:
Abstract
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.
PDB ID: 1JOYDownload
MMDB ID: 12462
PDB Deposition Date: 1998/12/28
Updated in MMDB: 2013/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 1JOY: dimeric; determined by author
Molecular Components in 1JOY
Label Count Molecule
Proteins (2 molecules)
2
Protein (Envz_ecoli)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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