1yfk

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{{Seed}}
 
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[[Image:1yfk.png|left|200px]]
 
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==Crystal structure of human B type phosphoglycerate mutase==
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The line below this paragraph, containing "STRUCTURE_1yfk", creates the "Structure Box" on the page.
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<StructureSection load='1yfk' size='340' side='right'caption='[[1yfk]], [[Resolution|resolution]] 2.70&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'>[[1yfk]] 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=1YFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YFK 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]] 2.7&#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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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{{STRUCTURE_1yfk| PDB=1yfk | 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=1yfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfk OCA], [https://pdbe.org/1yfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yfk RCSB], [https://www.ebi.ac.uk/pdbsum/1yfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PGAM1_HUMAN PGAM1_HUMAN] Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
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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/yf/1yfk_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=1yfk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as the cofactor. The crystal structures of human dPGM-B bound with citrate were determined in two crystal forms. These structures reveal a dimerization mode conserved in both of dPGM and BPGM (bisphosphoglycerate mutase), based on which a dPGM/BPGM heterodimer structure is proposed. Structural comparison supports that the conformational changes of residues 13-21 and 98-117 determine PGM/BPGM activity differences. The citrate-binding mode suggests a substrate-binding model, consistent with the structure of Escherichia coli dPGM/vanadate complex. A chloride ion was found in the center of the dimer, providing explanation for the contribution of chloride ion to dPGM activities. Based on the structural information, the possible reasons for the deficient human dPGM mutations found in some patients are also discussed.
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===Crystal structure of human B type phosphoglycerate mutase===
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Crystal structure of human B-type phosphoglycerate mutase bound with citrate.,Wang Y, Wei Z, Liu L, Cheng Z, Lin Y, Ji F, Gong W Biochem Biophys Res Commun. 2005 Jun 17;331(4):1207-15. PMID:15883004<ref>PMID:15883004</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1yfk" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15883004}}, adds the Publication Abstract to the page
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*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15883004 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15883004}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1YFK 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=1YFK OCA].
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==Reference==
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Crystal structure of human B-type phosphoglycerate mutase bound with citrate., Wang Y, Wei Z, Liu L, Cheng Z, Lin Y, Ji F, Gong W, Biochem Biophys Res Commun. 2005 Jun 17;331(4):1207-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15883004 15883004]
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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: Alpha/beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:18:38 2008''
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Current revision

Crystal structure of human B type phosphoglycerate mutase

PDB ID 1yfk

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