1php
From Proteopedia
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STRUCTURE OF THE ADP COMPLEX OF THE 3-PHOSPHOGLYCERATE KINASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.65 ANGSTROMS
Overview
The structure of the ADP complex of the enzyme 3-phosphoglycerate kinase, (PGK, E.C. 2.7.2.3) from Bacillus stearothermophilus NCA-1503 has been, determined by the method of molecular replacement. The structure has been, refined to an R factor of 0.16 for all data between 10.0 and 1.65 A, resolution, using data collected on the Hendrix-Lentfer imaging plate at, the EMBL outstation in Hamburg. The r.m.s. deviations from stereochemical, ideality are 0.010 and 0.011 A for bonds and planes, respectively., Although crystallized in the presence of the nucleotide product MgATP, the, high-resolution structure reveals the bound nucleotide to be MgADP, reflecting the low intrinsic ATPase activity of PGK. Although the two, domains of this enzyme are found to be some 4.5 degrees closer together, than is found in the yeast and horse-muscle apo-enzyme structures, this, structure represents the 'open' rather than the 'closed', catalytically, competent form, of the enzyme.
About this Structure
1PHP is a Single protein structure of sequence from Geobacillus stearothermophilus with MG and ADP as ligands. Active as Phosphoglycerate kinase, with EC number 2.7.2.3 Full crystallographic information is available from OCA.
Reference
Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 A., Davies GJ, Gamblin SJ, Littlechild JA, Dauter Z, Wilson KS, Watson HC, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):202-9. PMID:15299460
Page seeded by OCA on Tue Nov 20 23:49:30 2007
