1J0X

Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)

Summary for 1J0X

• Entry DOI: 10.2210/pdb1j0x/pdb
• Descriptor: glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase, dehydrogenase, rossmann fold, mammalian gapdh, apoptosis, negative cooperativity
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cytoplasm, cytosol : P46406
• Total number of polymer chains: 4
• Total formula weight: 144349.91

Authors

Cowan-Jacob, S.W.,Kaufmann, M.,Anselmo, A.N.,Stark, W.,Grutter, M.G. (deposition date: 2002-11-25, release date: 2003-12-09, Last modification date: 2023-10-25)

Primary citation

Cowan-Jacob, S.W.,Kaufmann, M.,Anselmo, A.N.,Stark, W.,Grutter, M.G.
Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase.
Acta Crystallogr.,Sect.D, 59:2218-2227, 2003

PubMed Abstract: The crystal structure of the tetrameric form of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) isolated from rabbit muscle was solved at 2.4 A resolution after careful dynamic light-scattering experiments to find a suitable buffer for crystallization trials. The refined model has a crystallographic R factor of 20.3%. Here, the first detailed model of a mammalian GAPDH is presented. The cofactor NAD(+) (nicotinamide adenine dinucleotide) is bound to two subunits of the tetrameric enzyme, which is consistent with the negative cooperativity of NAD(+) binding to this enzyme. The structure of rabbit-muscle GAPDH is of interest because it shares 91% sequence identity with the human enzyme; human GAPDH is a potential target for the development of anti-apoptotic drugs. In addition, differences in the cofactor-binding pocket compared with the homology-model structure of GAPDH from the malaria parasite Plasmodium falciparum could be exploited in order to develop novel selective and potential antimalaria drugs.

PubMed: 14646080
DOI: 10.1107/S0907444903020493

Experimental method

X-RAY DIFFRACTION (2.4 Å)