1CHN
MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE
Summary for 1CHN
| Entry DOI | 10.2210/pdb1chn/pdb |
| Descriptor | CHEY, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | signal transduction protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 14005.44 |
| Authors | Bellsolell, L.,Coll, M. (deposition date: 1994-04-20, release date: 1994-07-31, Last modification date: 2024-02-07) |
| Primary citation | Bellsolell, L.,Prieto, J.,Serrano, L.,Coll, M. Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. J.Mol.Biol., 238:489-495, 1994 Cited by PubMed Abstract: The three-dimensional crystal structure of the bacterial chemotaxis protein CheY with the essential Mg2+ cation bound to the active site reveals large conformational changes caused by the metal binding. Displacements of up to 10 A are observed in several residues at the N terminus of alpha-helix 4 and in the preceding loop. One turn of this helix unwinds, and an Asn residue that was located inside the helix becomes the new N-cap. This supports the important role that N or C-cap residues play in alpha-helix stability. In addition the preceding beta-strand becomes elongated and a new beta-turn appears. The final effect is a significant modification of the surface relief of the protein in a region previously indicated, by genetic analysis, to be essential for CheY function. It is suggested that binding of a divalent cation to CheY could play a significant part in CheY activation and consequently in signal transduction in prokaryotes. PubMed: 8176739DOI: 10.1006/jmbi.1994.1308 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
Download full validation report
