View source for 4y6n


==Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-1==
<StructureSection load='4y6n' size='340' side='right'caption='[[4y6n]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4y6n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y6N 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]] 2.348&#8491;</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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</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=4y6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y6n OCA], [https://pdbe.org/4y6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y6n RCSB], [https://www.ebi.ac.uk/pdbsum/4y6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y6n ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== Publication Abstract from PubMed ==
Glycosyltransferases (GTs) comprise a prominent family of enzymes that play critical roles in a variety of cellular processes, including cell signaling, cell development, and host-pathogen interactions. Glycosyl transfer can proceed with either inversion or retention of the anomeric configuration with respect to the reaction substrates and products. The elucidation of the catalytic mechanism of retaining GTs remains a major challenge. A native ternary complex of a GT in a productive mode for catalysis is reported, that of the retaining glucosyl-3-phosphoglycerate synthase GpgS from M. tuberculosis in the presence of the sugar donor UDP-Glc, the acceptor substrate phosphoglycerate, and the divalent cation cofactor. Through a combination of structural, chemical, enzymatic, molecular dynamics, and quantum-mechanics/molecular-mechanics (QM/MM) calculations, the catalytic mechanism was unraveled, thereby providing a strong experimental support for a front-side substrate-assisted SN i-type reaction.

A Native Ternary Complex Trapped in a Crystal Reveals the Catalytic Mechanism of a Retaining Glycosyltransferase.,Albesa-Jove D, Mendoza F, Rodrigo-Unzueta A, Gomollon-Bel F, Cifuente JO, Urresti S, Comino N, Gomez H, Romero-Garcia J, Lluch JM, Sancho-Vaello E, Biarnes X, Planas A, Merino P, Masgrau L, Guerin ME Angew Chem Int Ed Engl. 2015 Jul 1. doi: 10.1002/anie.201504617. PMID:26136334<ref>PMID:26136334</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4y6n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Albesa-Jove D]]
[[Category: Cifuente JO]]
[[Category: Comino N]]
[[Category: Guerin ME]]
[[Category: Rodrigo-Unzueta A]]
[[Category: Sancho-Vaello E]]
[[Category: Urresti S]]