4my4: Difference between revisions
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The | ==Crystal structure of phosphoglycerate mutase from Staphylococcus aureus.== | ||
<StructureSection load='4my4' size='340' side='right'caption='[[4my4]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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='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> | |||
</table> | |||
== Function == | |||
[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;"> | |||
== 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<ref>PMID:25611430</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4my4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]] | |||
[[Category: Bose M]] | |||
[[Category: Das AK]] | |||
[[Category: Gujar A]] | |||
[[Category: Kundu A]] | |||
[[Category: Roychowdhury A]] | |||
Latest revision as of 17:44, 8 November 2023
Crystal structure of phosphoglycerate mutase from Staphylococcus aureus.Crystal structure of phosphoglycerate mutase from Staphylococcus aureus.
Structural highlights
FunctionQ2G029_STAA8 Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).[HAMAP-Rule:MF_01038][SAAS:SAAS011258_004_004839] Publication Abstract from PubMedCofactor-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 AlsoReferences
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