1I5N
Crystal structure of the P1 domain of CheA from Salmonella typhimurium
Summary for 1I5N
| Entry DOI | 10.2210/pdb1i5n/pdb |
| Descriptor | CHEMOTAXIS PROTEIN CHEA, SULFATE ION (3 entities in total) |
| Functional Keywords | four-helix bundle, transferase |
| Biological source | Salmonella typhimurium |
| Total number of polymer chains | 4 |
| Total formula weight | 67707.15 |
| Authors | Mourey, L.,Da Re, S.,Pedelacq, J.-D.,Tolstyk, T.,Faurie, C.,Guillet, V.,Stock, J.B.,Samama, J.-P. (deposition date: 2001-02-28, release date: 2001-07-11, Last modification date: 2024-10-30) |
| Primary citation | Mourey, L.,Da Re, S.,Pedelacq, J.-D.,Tolstykh, T.,Faurie, C.,Guillet, V.,Stock, J.B.,Samama, J.-P. Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis J.Biol.Chem., 276:31074-31082, 2001 Cited by PubMed Abstract: 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. PubMed: 11387324DOI: 10.1074/jbc.M101943200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.14 Å) |
Structure validation
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