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| | ==Crystal structure of phosphoglycerate mutase from Staphylococcus aureus.== | | ==Crystal structure of phosphoglycerate mutase from Staphylococcus aureus.== |
| - | <StructureSection load='4my4' size='340' side='right' caption='[[4my4]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4my4' size='340' side='right'caption='[[4my4]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4my4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MY4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MY4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4my4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MY4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gpmI, SAOUHSC_00798 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93061 STAA8])</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=4my4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4my4 OCA], [https://pdbe.org/4my4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4my4 RCSB], [https://www.ebi.ac.uk/pdbsum/4my4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4my4 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] </span></td></tr>
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| - | <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=4my4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4my4 OCA], [http://pdbe.org/4my4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4my4 RCSB], [http://www.ebi.ac.uk/pdbsum/4my4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4my4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q2G029_STAA8 Q2G029_STAA8]] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).[HAMAP-Rule:MF_01038][SAAS:SAAS011258_004_004839] | + | [https://www.uniprot.org/uniprot/Q2G029_STAA8 Q2G029_STAA8] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).[HAMAP-Rule:MF_01038][SAAS:SAAS011258_004_004839] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Phosphoglycerate Mutase|Phosphoglycerate Mutase]] | + | *[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Phosphoglycerate mutase]] | + | [[Category: Large Structures]] |
| - | [[Category: Staa8]] | + | [[Category: Staphylococcus aureus subsp. aureus NCTC 8325]] |
| - | [[Category: Bose, M]] | + | [[Category: Bose M]] |
| - | [[Category: Das, A K]] | + | [[Category: Das AK]] |
| - | [[Category: Gujar, A]] | + | [[Category: Gujar A]] |
| - | [[Category: Kundu, A]] | + | [[Category: Kundu A]] |
| - | [[Category: Roychowdhury, A]] | + | [[Category: Roychowdhury A]] |
| - | [[Category: Cytosol]]
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| - | [[Category: Glycolytic enzyme]]
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| - | [[Category: Isomerase]]
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| Structural highlights
Function
Q2G029_STAA8 Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).[HAMAP-Rule:MF_01038][SAAS:SAAS011258_004_004839]
Publication Abstract from PubMed
Cofactor-independent phosphoglycerate mutase (iPGM), an important enzyme in glycolysis and gluconeogenesis, catalyses the isomerization of 2- and 3-phosphoglycerates by an Mn2+ -dependent phospho-transfer mechanism via a phospho-enzyme intermediate. Crystal structures of bi-domain iPGM from Staphylococcus aureus, together with substrate-bound forms, have revealed a new conformation of the enzyme, representing an intermediate state of domain movement. The substrate-binding site and the catalytic site are present in two distinct domains in the intermediate form. X-ray crystallography complemented by simulated dynamics has enabled delineation of the complete catalytic cycle, which includes binding of the substrate, followed by its positioning into the catalytic site, phospho-transfer and finally product release. The present work describes a novel mechanism of domain movement controlled by a hydrophobic patch that is exposed on domain closure and acts like a spring to keep the protein in open conformation. Domain closing occurs after substrate binding, and is essential for phospho-transfer, whereas the open conformation is a prerequisite for efficient substrate binding and product dissociation. A new model of catalysis has been proposed by correlating the hinge-bending motion with the phospho-transfer mechanism.
Complete catalytic cycle of cofactor-independent phosphoglycerate mutase involves a spring-loaded mechanism.,Roychowdhury A, Kundu A, Bose M, Gujar A, Mukherjee S, Das AK FEBS J. 2015 Jan 22. doi: 10.1111/febs.13205. PMID:25611430[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Roychowdhury A, Kundu A, Bose M, Gujar A, Mukherjee S, Das AK. Complete catalytic cycle of cofactor-independent phosphoglycerate mutase involves a spring-loaded mechanism. FEBS J. 2015 Jan 22. doi: 10.1111/febs.13205. PMID:25611430 doi:http://dx.doi.org/10.1111/febs.13205
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