4my4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==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 [ | <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><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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Phosphoglycerate | *[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus subsp. aureus NCTC 8325]] | ||
[[Category: Bose | [[Category: Bose M]] | ||
[[Category: Das | [[Category: Das AK]] | ||
[[Category: Gujar | [[Category: Gujar A]] | ||
[[Category: Kundu | [[Category: Kundu A]] | ||
[[Category: Roychowdhury | [[Category: Roychowdhury A]] | ||
Revision as of 13:18, 28 December 2022
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
|
| ||||||||||||||||