13PK

TERNARY COMPLEX OF PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI

Summary for 13PK

• Entry DOI: 10.2210/pdb13pk/pdb
• Descriptor: 3-PHOSPHOGLYCERATE KINASE, MAGNESIUM ION, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: kinase, phosphoglycerate, ternary complex, glycolysis, transferase
• Biological source: Trypanosoma brucei
• Cellular location: Glycosome: P07378
• Total number of polymer chains: 4
• Total formula weight: 181547.90

Authors

Bernstein, B.E.,Michels, P.A.M.,Hol, W.G.J. (deposition date: 1996-11-23, release date: 1997-12-24, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)