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| | ==Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA== | | ==Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA== |
| - | <StructureSection load='5jqx' size='340' side='right' caption='[[5jqx]], [[Resolution|resolution]] 2.82Å' scene=''> | + | <StructureSection load='5jqx' size='340' side='right'caption='[[5jqx]], [[Resolution|resolution]] 2.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jqx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycta Mycta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jqx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Ra Mycobacterium tuberculosis H37Ra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JQX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</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]] 2.82Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jqq|5jqq]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gpgS, Rv1208 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=419947 MYCTA])</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=5jqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqx OCA], [https://pdbe.org/5jqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jqx RCSB], [https://www.ebi.ac.uk/pdbsum/5jqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqx 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/Glucosyl-3-phosphoglycerate_synthase Glucosyl-3-phosphoglycerate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.266 2.4.1.266] </span></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=5jqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqx OCA], [http://pdbe.org/5jqx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jqx RCSB], [http://www.ebi.ac.uk/pdbsum/5jqx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GPGS_MYCTU GPGS_MYCTU]] Involved in the biosynthesis of methylglucose lipopolysaccharides (MGLPs). Catalyzes the condensation of NDP-glucose and 3-phospho-glycerate (3-PGA) to yield glucosyl-3-phosphoglycerate (GPG).<ref>PMID:22637481</ref> | + | [https://www.uniprot.org/uniprot/GPGS_MYCTU GPGS_MYCTU] Involved in the biosynthesis of methylglucose lipopolysaccharides (MGLPs). Catalyzes the condensation of NDP-glucose and 3-phospho-glycerate (3-PGA) to yield glucosyl-3-phosphoglycerate (GPG).<ref>PMID:22637481</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glucosyl-3-phosphoglycerate synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Mycta]] | + | [[Category: Mycobacterium tuberculosis H37Ra]] |
| - | [[Category: Albesa-Jove, D]] | + | [[Category: Albesa-Jove D]] |
| - | [[Category: Arrasate, P]] | + | [[Category: Arrasate P]] |
| - | [[Category: Carreras-Gonzalez, A]] | + | [[Category: Carreras-Gonzalez A]] |
| - | [[Category: Comino, N]] | + | [[Category: Comino N]] |
| - | [[Category: Guerin, M E]] | + | [[Category: Guerin ME]] |
| - | [[Category: Rodrigo-Unzueta, A]] | + | [[Category: Rodrigo-Unzueta A]] |
| - | [[Category: Sancho-Vaello, E]] | + | [[Category: Sancho-Vaello E]] |
| - | [[Category: Urresti, S]] | + | [[Category: Urresti S]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GPGS_MYCTU Involved in the biosynthesis of methylglucose lipopolysaccharides (MGLPs). Catalyzes the condensation of NDP-glucose and 3-phospho-glycerate (3-PGA) to yield glucosyl-3-phosphoglycerate (GPG).[1]
Publication Abstract from PubMed
Glycosyltransferases (GTs) play a central role in nature. They catalyze the transfer of a sugar moiety to a broad range of acceptor substrates. GTs are highly selective enzymes, allowing the recognition of subtle structural differences in the sequences and stereochemistry of their sugar and acceptor substrates. We report here a series of structural snapshots of the reaction center of the retaining glucosyl-3-phosphoglycerate synthase (GpgS). During this sequence of events, we visualize how the enzyme guides the substrates into the reaction center where the glycosyl transfer reaction takes place, and unveil the mechanism of product release, involving multiple conformational changes not only in the substrates/products but also in the enzyme. The structural data are further complemented by metadynamics free-energy calculations, revealing how the equilibrium of loop conformations is modulated along these itineraries. The information reported here represent an important contribution for the understanding of GT enzymes at the molecular level.
Structural Snapshots and Loop Dynamics along the Catalytic Cycle of Glycosyltransferase GpgS.,Albesa-Jove D, Romero-Garcia J, Sancho-Vaello E, Contreras FX, Rodrigo-Unzueta A, Comino N, Carreras-Gonzalez A, Arrasate P, Urresti S, Biarnes X, Planas A, Guerin ME Structure. 2017 Jul 5;25(7):1034-1044.e3. doi: 10.1016/j.str.2017.05.009. Epub, 2017 Jun 15. PMID:28625787[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Urresti S, Albesa-Jove D, Schaeffer F, Pham HT, Kaur D, Gest P, van der Woerd MJ, Carreras-Gonzalez A, Lopez-Fernandez S, Alzari PM, Brennan PJ, Jackson M, Guerin ME. Mechanistic insights into the retaining glucosyl-3-phosphoglycerate synthase from mycobacteria. J Biol Chem. 2012 May 25. PMID:22637481 doi:10.1074/jbc.M112.368191
- ↑ Albesa-Jove D, Romero-Garcia J, Sancho-Vaello E, Contreras FX, Rodrigo-Unzueta A, Comino N, Carreras-Gonzalez A, Arrasate P, Urresti S, Biarnes X, Planas A, Guerin ME. Structural Snapshots and Loop Dynamics along the Catalytic Cycle of Glycosyltransferase GpgS. Structure. 2017 Jul 5;25(7):1034-1044.e3. doi: 10.1016/j.str.2017.05.009. Epub, 2017 Jun 15. PMID:28625787 doi:http://dx.doi.org/10.1016/j.str.2017.05.009
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