1chn
From Proteopedia
|
MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE
Overview
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.
About this Structure
1CHN is a Single protein structure of sequence from Escherichia coli with MG as ligand. Full crystallographic information is available from OCA.
Reference
Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface., Bellsolell L, Prieto J, Serrano L, Coll M, J Mol Biol. 1994 May 13;238(4):489-95. PMID:8176739
Page seeded by OCA on Tue Nov 20 12:27:52 2007
