2hhj | pdb_00002hhj

Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate (15 days)

spinqualitylabelsall models 2hhj, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hhj is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: 3PG, DG2, HAI, NEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease PMGE_HUMAN Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis. Function PMGE_HUMAN Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoglycerate mutase 3D structures

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