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 ...
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.
Related Citations:
The Structure of a Thermally Stable 3-Phosphoglycerate Kinase and a Comparison with its Mesophilic Equivalent Davies, G.J., Gamblin, S.J., Littlechild, J.A., Watson, H.C. (1993) Proteins 15: 283
Purification, Crystallisation and Preliminary X-Ray Analysis of the 3-Phosphoglycerate Kinase from Bacillus Stearothermophilus Davies, G.J., Gamblin, S.J., Littlechild, J.A., Watson, H.C. (1992) J Mol Biol 227: 1263
Sequence and Expression of the Gene Encoding 3-Phosphoglycerate Kinase from Bacillus Stearothermophilus Davies, G.J., Littlechild, J.A., Watson, H.C., Hall, L. (1991) Gene 109: 39
Organizational Affiliation:
Department of Biochemistry, School of Medical Sciences, University of Bristol, England.
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