1JOY

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

Summary for 1JOY

• Entry DOI: 10.2210/pdb1joy/pdb
• Descriptor: PROTEIN (ENVZ_ECOLI) (1 entity in total)
• Functional Keywords: histidine kinase, sensory transduction, osmolarity sensor protein, inner membrane, phosphorylation, transferase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P02933
• Total number of polymer chains: 2
• Total formula weight: 15187.34

Authors

Tomomori, C.,Tanaka, T.,Dutta, R.,Park, H.,Saha, S.K.,Zhu, Y.,Ishima, R.,Liu, D.,Tong, K.I.,Kurokawa, H.,Qian, H.,Inouye, M.,Ikura, M. (deposition date: 1998-12-28, release date: 2000-01-12, Last modification date: 2023-12-27)

Primary citation

Tomomori, C.,Tanaka, T.,Dutta, R.,Park, H.,Saha, S.K.,Zhu, Y.,Ishima, R.,Liu, D.,Tong, K.I.,Kurokawa, H.,Qian, H.,Inouye, M.,Ikura, M.
Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ.
Nat.Struct.Biol., 6:729-734, 1999

PubMed 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.

PubMed: 10426948
DOI: 10.1038/11495

Experimental method

SOLUTION NMR