1VSV

Crystal Structure of holo-glyceraldehyde 3-phosphate dehydrogenase from Cryptosporidium parvum

Replaces:  3CIE

Summary for 1VSV

• Entry DOI: 10.2210/pdb1vsv/pdb
• Related: 1VSV 3CIF
• Descriptor: Glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: dehyrogenase, glycolysis, glycolytic enzyme, oxidoreductase
• Biological source: Cryptosporidium parvum
• Total number of polymer chains: 4
• Total formula weight: 155989.08

Authors

Cook, W.J.,Senkovich, O.,Chattopadhyay, D. (deposition date: 2008-03-11, release date: 2009-03-24, Last modification date: 2023-08-23)

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

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: 19243605
DOI: 10.1186/1472-6807-9-9

Experimental method

X-RAY DIFFRACTION (2 Å)