View source for 4my4


==Crystal structure of phosphoglycerate mutase from Staphylococcus aureus.==
<StructureSection load='4my4' size='340' side='right'caption='[[4my4]], [[Resolution|resolution]] 2.00&Aring;' 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]] 2&#8491;</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&reg;/PubMed&reg;, 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]]