3CIF
Crystal Structure of C153S mutant glyceraldehyde 3-phosphate dehydrogenase from Cryptosporidium parvum
Summary for 3CIF
| Entry DOI | 10.2210/pdb3cif/pdb |
| Related | 1VSU 1VSV |
| Descriptor | Glyceraldehyde-3-phosphate dehydrogenase, GLYCERALDEHYDE-3-PHOSPHATE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | dehyrogenase glyceraldehyde 3-phosphate, glycolysis, glycolytic enzyme, oxidoreductase |
| Biological source | Cryptosporidium parvum |
| Total number of polymer chains | 4 |
| Total formula weight | 156701.78 |
| Authors | Cook, W.J.,Senkovich, O.,Chattopadhyay, D. (deposition date: 2008-03-11, release date: 2009-03-24, Last modification date: 2023-08-30) |
| Primary citation | Cook, W.J.,Senkovich, O.,Chattopadhyay, D. An unexpected phosphate binding site in Glyceraldehyde 3-Phosphate Dehydrogenase: Crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzyme BMC STRUCT.BIOL., 9:9-9, 2009 Cited by PubMed Abstract: The structure, function and reaction mechanism of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) have been extensively studied. Based on these studies, three anion binding sites have been identified, one 'Ps' site (for binding the C-3 phosphate of the substrate) and two sites, 'Pi' and 'new Pi', for inorganic phosphate. According to the original flip-flop model, the substrate phosphate group switches from the 'Pi' to the 'Ps' site during the multistep reaction. In light of the discovery of the 'new Pi' site, a modified flip-flop mechanism, in which the C-3 phosphate of the substrate binds to the 'new Pi' site and flips to the 'Ps' site before the hydride transfer, was proposed. An alternative model based on a number of structures of B. stearothermophilus GAPDH ternary complexes (non-covalent and thioacyl intermediate) proposes that in the ternary Michaelis complex the C-3 phosphate binds to the 'Ps' site and flips from the 'Ps' to the 'new Pi' site during or after the redox step. PubMed: 19243605DOI: 10.1186/1472-6807-9-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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