1PHP

STRUCTURE OF THE ADP COMPLEX OF THE 3-PHOSPHOGLYCERATE KINASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.65 ANGSTROMS

Summary for 1PHP

• Entry DOI: 10.2210/pdb1php/pdb
• Descriptor: 3-PHOSPHOGLYCERATE KINASE, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: kinase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 43241.53

Authors

Davies, G.J.,Watson, H.C. (deposition date: 1994-04-12, release date: 1994-06-22, Last modification date: 2024-02-14)

Primary citation

Davies, G.J.,Gamblin, S.J.,Littlechild, J.A.,Dauter, Z.,Wilson, K.S.,Watson, H.C.
Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 A.
Acta Crystallogr.,Sect.D, 50:202-209, 1994

PubMed Abstract: 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.

PubMed: 15299460
DOI: 10.1107/S0907444993011138

Experimental method

X-RAY DIFFRACTION (1.65 Å)