Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

Lionel Mourey, Sandra Da Re, Jean Denis Pédelacq, Tatiana Tolstykh, Cécile Faurie, Valérie Guillet, Jeffry Benton Stock, Jean Pierre Samama

Research output: Contribution to journalArticle

67 Scopus citations

Abstract

The x-ray crystal structure of the P1 or H domain of the Salmonella CheA protein has been solved at 2.1-Å resolution. The structure is composed of an up-down up-down four-helix bundle that is typical of histidine phosphotransfer or HPt domains such as Escherichia coli ArcBC and Saccharomyces cerevisiae Ypd1. Loop regions and additional structural features distinguish all three proteins. The CheA domain has an additional C-terminal helix that lies over the surface formed by the C and D helices. The phosphoaccepting His-48 is located at a solvent-exposed position in the middle of the B helix where it is surrounded by several residues that are characteristic of other HPt domains. Mutagenesis studies indicate that conserved glutamate and lysine residues that are part of a hydrogen-bond network with His-48 are essential for the ATP-dependent phosphorylation reaction but not for the phosphotransfer reaction with CheY. These results suggest that the CheA-P1 domain may serve as a good model for understanding the general function of HPt domains in complex two-component phosphorelay systems.

Original languageEnglish (US)
Pages (from-to)31074-31082
Number of pages9
JournalJournal of Biological Chemistry
Volume276
Issue number33
DOIs
StatePublished - Aug 17 2001

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Medicine(all)
  • Molecular Biology
  • Cell Biology

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