2f90

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[[Image:2f90.jpg|left|200px]]<br /><applet load="2f90" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2f90, resolution 2.00&Aring;" />
 
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'''Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and AlF4-'''<br />
 
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==Overview==
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==Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and AlF4-==
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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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<StructureSection load='2f90' size='340' side='right'caption='[[2f90]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2f90]] 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=2F90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F90 FirstGlance]. <br>
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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>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene></td></tr>
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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=2f90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f90 OCA], [https://pdbe.org/2f90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f90 RCSB], [https://www.ebi.ac.uk/pdbsum/2f90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f90 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/f9/2f90_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=2f90 ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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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]]
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*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2F90 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=ALF:'>ALF</scene> and <scene name='pdbligand=3PG:'>3PG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F90 OCA].
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__TOC__
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17052986 17052986]
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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: Liu, L.]]
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[[Category: Liu L]]
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[[Category: Wang, Y.]]
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[[Category: Wang Y]]
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[[Category: Wei, Z.]]
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[[Category: Wei Z]]
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[[Category: 3PG]]
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[[Category: ALF]]
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[[Category: bisphosphoglycerate mutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:24:51 2008''
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Current revision

Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and AlF4-

PDB ID 2f90

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