3chy
From Proteopedia
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CRYSTAL STRUCTURE OF ESCHERICHIA COLI CHEY REFINED AT 1.7-ANGSTROM RESOLUTION
Overview
The three-dimensional structure of wild-type CheY from Escherichia coli, has been refined by stereochemically restrained least squares minimization, to a crystallographic R-factor of 15.1% at 1.7-A resolution. The structure, contains 1165 atoms, including all atoms of the protein, 147 water, molecules, and three sulfate ions. The final model has root mean square, deviations of 0.018 and 0.049 A from idealized bond lengths and angle, distances, respectively. Seven amino acid side chains have been modeled in, dual conformations. CheY folds as a compact (beta/alpha)5 globular, protein, with the phosphorylation region contained in a cavity on one face, of the molecule. This active site area is bordered by the carboxyl termini, of the three central beta-strands, by alpha 1, and by the loop connecting, beta 5 to alpha 5. The Lys-109 side chain of this loop extends into the, active site by virtue of its cis peptide bond conformation preceding, Pro-110. The epsilon-amino group of Lys-109 is in close bonding contact, with the carboxyl group of Asp-57, the residue that is phosphorylated in, the activation process of CheY. The details of the hydrogen bonding, network in the phosphorylation region indicate that structural, rearrangements must accompany the phosphorylation of Asp-57.
About this Structure
3CHY is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution., Volz K, Matsumura P, J Biol Chem. 1991 Aug 15;266(23):15511-9. PMID:1869568
Page seeded by OCA on Tue Nov 20 19:34:34 2007
