2f90

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spinqualitylabelsall models 2f90, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and AlF4-

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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.

Disease

Known disease associated with this structure: Hemolytic anemia due to bisphosphoglycerate mutase deficiency OMIM:[222800]

About this Structure

2F90 is a Single protein structure of sequence from Homo sapiens with ALF and 3PG as ligands. 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 Mon Nov 12 22:01:37 2007