1i5n
From Proteopedia
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Crystal structure of the P1 domain of CheA from Salmonella typhimurium
Overview
The x-ray crystal structure of the P1 or H domain of the Salmonella CheA, protein has been solved at 2.1-A 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.
About this Structure
1I5N is a Single protein structure of sequence from Salmonella typhimurium with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis., Mourey L, Da Re S, Pedelacq JD, Tolstykh T, Faurie C, Guillet V, Stock JB, Samama JP, J Biol Chem. 2001 Aug 17;276(33):31074-82. Epub 2001 May 31. PMID:11387324
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