2a9j
From Proteopedia
(New page: 200px<br /> <applet load="2a9j" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a9j, resolution 2.00Å" /> '''Human bisphosphogly...) |
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| - | [[Image:2a9j. | + | [[Image:2a9j.jpg|left|200px]]<br /><applet load="2a9j" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2a9j" size=" | + | |
caption="2a9j, resolution 2.00Å" /> | caption="2a9j, resolution 2.00Å" /> | ||
'''Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)'''<br /> | '''Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)'''<br /> | ||
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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== | ||
| - | 2A9J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with 3PG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Bisphosphoglycerate_mutase Bisphosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.4 5.4.2.4] Full crystallographic information is available from [http:// | + | 2A9J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=3PG:'>3PG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Bisphosphoglycerate_mutase Bisphosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.4 5.4.2.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: bisphosphoglycerate mutase]] | [[Category: bisphosphoglycerate mutase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:18:10 2008'' |
Revision as of 13:18, 23 January 2008
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Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)
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
2A9J is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Bisphosphoglycerate mutase, with EC number 5.4.2.4 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
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