13PK

TERNARY COMPLEX OF PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI

13PK の概要

• エントリーDOI: 10.2210/pdb13pk/pdb
• 分子名称: 3-PHOSPHOGLYCERATE KINASE, MAGNESIUM ION, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: kinase, phosphoglycerate, ternary complex, glycolysis, transferase
• 由来する生物種: Trypanosoma brucei
• 細胞内の位置: Glycosome: P07378
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 181547.90

構造登録者

Bernstein, B.E.,Michels, P.A.M.,Hol, W.G.J. (登録日: 1996-11-23, 公開日: 1997-12-24, 最終更新日: 2024-05-22)

主引用文献

Bernstein, B.E.,Michels, P.A.,Hol, W.G.
Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation.
Nature, 385:275-278, 1997

PubMed Abstract: Phosphoglycerate kinase (PGK), a key enzyme in glycolysis, catalyses the transfer of a phosphoryl-group from 1,3-bisphosphoglycerate to ADP to form 3-phosphoglycerate and ATP. Despite extensive kinetic and structural investigations over more than two decades, the conformation assumed by this enzyme during catalysis remained unknown. Here we present the 2.8 A crystal structure of a ternary complex of PGK from Trypanosoma brucei, the causative agent of sleeping sickness. This structure determination relied on a procedure in which fragments containing less than 10% of the scattering mass were successively positioned in the unit cell to obtain phases. The PGK ternary complex exhibits a dramatic closing of the large cleft between the two domains seen in all previous studies, thereby bringing the two ligands, 3-phosphoglycerate and ADP into close proximity. Our results demonstrate that PGK is a hinge-bending enzyme, reveal a novel mechanism in which substrate-induced effects combine synergistically to induce major conformational changes and, to our knowledge, afford the first observation of the PGK active site in a catalytic conformation.

PubMed: 9000079
DOI: 10.1038/385275a0

実験手法

X-RAY DIFFRACTION (2.5 Å)