Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme
- 1 June 1979
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 279 (5716), 773-777
- https://doi.org/10.1038/279773a0
Abstract
The fitting of sequenced peptides to a high-resolution X-ray map of phosphoglycerate kinase has yielded the complete sequence and structure of the horse muscle enzyme. Metal ADP and ATP substrates are bound to one of the two widely separated domains in an environment that seems unsuitable for phosphoglycerate binding. The most plausible binding site for the phosphoglycerate substrate is on the other domain about 10 Å from the ATP, which implies the possibility of a large scale hinge-bending of the domains to bring the two substrates together in a water-free environment for catalysis.This publication has 23 references indexed in Scilit:
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