1SZJ

STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE FROM PALINURUS VERSICOLOR REFINED 2.0 ANGSTROM RESOLUTION

Summary for 1SZJ

• Entry DOI: 10.2210/pdb1szj/pdb
• Descriptor: D-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE, SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, d-glyceraldehyde-3-phosphate-dehydrogenase, molecular symmetry, allosterism
• Biological source: Palinurus versicolor (South China Sea lobster)
• Cellular location: Cytoplasm: P56649
• Total number of polymer chains: 2
• Total formula weight: 73245.11

Authors

Song, S.,Li, J.,Lin, Z. (deposition date: 1997-02-04, release date: 1998-09-16, Last modification date: 2024-04-03)

Primary citation

Song, S.Y.,Gao, Y.G.,Zhou, J.M.,Tsou, C.L.
Preliminary crystallographic studies of lobster D-glyceraldehyde-3-phosphate dehydrogenase and the modified enzyme carrying the fluorescent derivative.
J.Mol.Biol., 171:225-228, 1983

PubMed Abstract: When the active-site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase is irradiated with ultraviolet light in the presence of NAD+, a fluorescent NAD derivative that is covalently linked to the enzyme is obtained. A preliminary crystallographic study of this fluorescent derivative, as well as of the native and the carboxymethylated enzymes from Palinurus versicolor, showed that they are isomorphous and belong to space group C2 as reported for the native enzyme from Palinurus vulgaris. The three forms of the enzyme, although they have identical unit cell parameters, differ considerably in their diffraction patterns, indicating marked differences in conformation in spite of the fact that they differ chemically only in a restricted region around the active site.

PubMed: 6655693
DOI: 10.1016/S0022-2836(83)80355-6

Experimental method

X-RAY DIFFRACTION (2 Å)