2F90

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

Summary for 2F90

• Entry DOI: 10.2210/pdb2f90/pdb
• Related: 1T8P
• Descriptor: Bisphosphoglycerate mutase, TETRAFLUOROALUMINATE ION, 3-PHOSPHOGLYCERIC ACID, ... (4 entities in total)
• Functional Keywords: bisphosphoglycerate mutase, isomerase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 62814.81

Authors

Wang, Y.,Liu, L.,Wei, Z.,Gong, W. (deposition date: 2005-12-05, release date: 2006-10-24, Last modification date: 2024-03-13)

Primary citation

Wang, Y.,Liu, L.,Wei, Z.,Cheng, Z.,Lin, Y.,Gong, W.
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase
J.Biol.Chem., 281:39642-39648, 2006

PubMed 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.

PubMed: 17052986
DOI: 10.1074/jbc.M606421200

Experimental method

X-RAY DIFFRACTION (2 Å)