2a9j
From Proteopedia
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Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)
Overview
Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a, series of intermolecular phosphoryl group transfer reactions. Its main, function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector, of hemoglobin. In this paper, we directly observed real-time motion of the, enzyme active site and the substrate during phosphoryl transfer. A series, of high resolution crystal structures of human bisphosphoglycerate mutase, co-crystallized with 2,3-bisphosphoglycerate, representing different time, points in the phosphoryl transfer reaction, were solved. These structures, not only clarify the argument concerning the substrate binding mode for, this enzyme family but also depict the entire process of the key histidine, phosphorylation as a "slow movie". It was observed that the enzyme, conformation continuously changed during the different states of the, reaction. These results provide direct evidence for an "in line", phosphoryl transfer mechanism, and the roles of some key residues in the, phosphoryl transfer process are identified.
About this Structure
2A9J is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Bisphosphoglycerate mutase, with EC number 5.4.2.4 Full crystallographic information is available from OCA.
Reference
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase., Wang Y, Liu L, Wei Z, Cheng Z, Lin Y, Gong W, J Biol Chem. 2006 Dec 22;281(51):39642-8. Epub 2006 Oct 18. PMID:17052986
Page seeded by OCA on Wed Jan 23 15:18:10 2008
