2a9j

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[[Image:2a9j.jpg|left|200px]]
 
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==Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)==
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The line below this paragraph, containing "STRUCTURE_2a9j", creates the "Structure Box" on the page.
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<StructureSection load='2a9j' size='340' side='right'caption='[[2a9j]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2a9j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A9J FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene></td></tr>
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{{STRUCTURE_2a9j| PDB=2a9j | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a9j OCA], [https://pdbe.org/2a9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a9j RCSB], [https://www.ebi.ac.uk/pdbsum/2a9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a9j ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/PMGE_HUMAN PMGE_HUMAN] Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:[https://omim.org/entry/222800 222800]. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.<ref>PMID:2542247</ref> <ref>PMID:1421379</ref> <ref>PMID:15054810</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/PMGE_HUMAN 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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a9/2a9j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a9j ConSurf].
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<div style="clear:both"></div>
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'''Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)'''
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==See Also==
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*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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2A9J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9J OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17052986 17052986]
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[[Category: Bisphosphoglycerate mutase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gong, W.]]
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[[Category: Gong W]]
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[[Category: Wang, Y.]]
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[[Category: Wang Y]]
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[[Category: 3-phosphoglycerate]]
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[[Category: Bisphosphoglycerate mutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:46:55 2008''
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Current revision

Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)

PDB ID 2a9j

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