ISDA: 1J0X

Deposition Date 2002-11-25

Release Date 2003-12-09

Last Version Date 2023-10-25

Entry Detail

PDB ID:

1J0X

Keywords:

OXIDOREDUCTASE

Title:

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

Biological Source:

Source Organism(s):

Oryctolagus cuniculus (Taxon ID: 9986)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.40 Å

R-Value Free:

0.23

R-Value Work:

0.20

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:glyceraldehyde-3-phosphate de
Gene (Uniprot):GAPDH
Chain IDs:A (auth: O), B (auth: P), C (auth: Q), D (auth: R)
Chain Length:332
Number of Molecules:4
Biological Source:Oryctolagus cuniculus

UniProt ID:P46406 Pfam ID:PF00044, PF02800 EC:1.2.1.12

Modified Residue

Compound ID	Chain ID	Parent Comp ID	Details	2D Image
CSX	A	CYS	S-OXY CYSTEINE

Ligand Molecules

NAD

Primary Citation

Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase.

Cowan-Jacob, S.W, Kaufmann, M, Anselmo, A.N, Stark, W, Grutter, M.G.Show

Acta Crystallogr. D Biol. Crystallogr. 59 2218 2227 (2003)

PMID: 14646080 DOI: 10.1107/S0907444903020493

Abstact

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.

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Primary Citation of related structures

Abstact

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