2f90
From Proteopedia
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|PDB= 2f90 |SIZE=350|CAPTION= <scene name='initialview01'>2f90</scene>, resolution 2.00Å | |PDB= 2f90 |SIZE=350|CAPTION= <scene name='initialview01'>2f90</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1t8p|1T8P]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f90 OCA], [http://www.ebi.ac.uk/pdbsum/2f90 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f90 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Hemolytic anemia due to bisphosphoglycerate mutase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=222800 222800]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
[[Category: Wei, Z.]] | [[Category: Wei, Z.]] | ||
| - | [[Category: 3PG]] | ||
| - | [[Category: ALF]] | ||
[[Category: bisphosphoglycerate mutase]] | [[Category: bisphosphoglycerate mutase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:59:34 2008'' |
Revision as of 23:59, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1T8P
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and AlF4-
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.
About this Structure
2F90 is a Single protein structure of sequence from Homo sapiens. 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 Mar 31 02:59:34 2008
