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2H4Z

Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate

Summary for 2H4Z
Entry DOI10.2210/pdb2h4z/pdb
Related2H4X 2H52
DescriptorBisphosphoglycerate mutase, (2R)-2,3-diphosphoglyceric acid (3 entities in total)
Functional Keywordsbisphosphoglycerate mutase, 2, 3-bisphosphoglycerate, isomerase
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight62768.82
Authors
Wang, Y.,Gong, W. (deposition date: 2006-05-25, release date: 2006-10-24, Last modification date: 2023-10-25)
Primary citationWang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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