Seeing the Process of Histidine Phosphorylation in Human Bisphosphoglycerate Mutase.
From: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
The Journal of biological chemistry
- Publish Date: Dec 2006
- ISSN: 0021-9258
- Volume: 281
- Issue: 51
- Pages: 39642-8
- Medium: Print
- Language: English
- Citation (JAMA): Wang Yanli, Liu Lin, Wei Zhiyi, et al. Seeing the Process of Histidine Phosphorylation in Human Bisphosphoglycerate Mutase.. J. Biol. Chem. Dec 2006;281:39642-8
Abstract
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.
Mesh Headings (Keywords): 2,3-Diphosphoglycerate, Allosteric Site, Binding Sites, Bisphosphoglycerate Mutase, Electrons, Hemoglobins, Histidine, Humans, Ligands, Models, Chemical, Models, Molecular, Phosphorylation, Protein Binding, Protein Structure, Tertiary, Substrate Specificity
Check for Full Text / PubMed Unique Identifier (PMID): 17052986
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.