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| | <StructureSection load='1yjx' size='340' side='right'caption='[[1yjx]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1yjx' size='340' side='right'caption='[[1yjx]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yjx]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YJX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yjx]] is a 12 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=1YJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YJX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yfk|1yfk]]</td></tr> | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjx OCA], [http://pdbe.org/1yjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yjx RCSB], [http://www.ebi.ac.uk/pdbsum/1yjx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjx ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjx OCA], [https://pdbe.org/1yjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yjx RCSB], [https://www.ebi.ac.uk/pdbsum/1yjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gong, W]] | + | [[Category: Gong W]] |
| - | [[Category: Liu, L]] | + | [[Category: Liu L]] |
| - | [[Category: Wang, Y]] | + | [[Category: Wang Y]] |
| - | [[Category: Wei, Z]] | + | [[Category: Wei Z]] |
| - | [[Category: Alpha/beta]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang Y, Wei Z, Liu L, Cheng Z, Lin Y, Ji F, Gong W. Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Biochem Biophys Res Commun. 2005 Jun 17;331(4):1207-15. PMID:15883004 doi:10.1016/j.bbrc.2005.03.243
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