1SZJ

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

1SZJ の概要

• エントリーDOI: 10.2210/pdb1szj/pdb
• 分子名称: D-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE, SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, d-glyceraldehyde-3-phosphate-dehydrogenase, molecular symmetry, allosterism
• 由来する生物種: Palinurus versicolor (South China Sea lobster)
• 細胞内の位置: Cytoplasm: P56649
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73245.11

構造登録者

Song, S.,Li, J.,Lin, Z. (登録日: 1997-02-04, 公開日: 1998-09-16, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)