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 Cited by 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: 10426948DOI: 10.1038/11495 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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