Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Journal of Biological Chemistry Année : 2001

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

Sandra da Re
  • Fonction : Auteur
Tatiana Tolstykh
  • Fonction : Auteur
Cécile Faurie
  • Fonction : Auteur
Jeffry B Stock
  • Fonction : Auteur
Jean-Pierre Samama
  • Fonction : Auteur

Résumé

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 ArcB C 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.
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Dates et versions

hal-03004208 , version 1 (20-11-2020)

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Lionel Mourey, Sandra da Re, Jean-Denis Pedelacq, Tatiana Tolstykh, Cécile Faurie, et al.. Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis. Journal of Biological Chemistry, 2001, 276, pp.31074 - 31082. ⟨10.1074/jbc.m101943200⟩. ⟨hal-03004208⟩
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