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PMID:10426948
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| Citation |
Tomomori, C, Tanaka, T, Dutta, R, Park, H, Saha, SK, Zhu, Y, Ishima, R, Liu, D, Tong, KI, Kurokawa, H, Qian, H, Inouye, M and Ikura, M (1999) Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. Nat. Struct. Biol. 6:729-34 |
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| 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. |
| Links |
PubMed Online version:10.1038/11495 |
| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Escherichia coli/enzymology; Escherichia coli Proteins; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Protein Conformation; Sequence Homology, Amino Acid; Solutions |
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