View source for 5vcs


==Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase with Bound Acceptor==
<StructureSection load='5vcs' size='340' side='right'caption='[[5vcs]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vcs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VCS 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]] 2.799&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5vcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vcs OCA], [https://pdbe.org/5vcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vcs RCSB], [https://www.ebi.ac.uk/pdbsum/5vcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vcs ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/MGAT2_HUMAN MGAT2_HUMAN] MGAT2-CDG. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/MGAT2_HUMAN MGAT2_HUMAN] Catalyzes an essential step in the conversion of oligo-mannose to complex N-glycans.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Asn-linked oligosaccharides are extensively modified during transit through the secretory pathway, first by trimming of the nascent glycan chains and subsequently by initiating and extending multiple oligosaccharide branches from the trimannosyl glycan core. Trimming and branching pathway steps are highly ordered and hierarchal based on the precise substrate specificities of the individual biosynthetic enzymes. A key committed step in the synthesis of complex-type glycans is catalyzed by N-acetylglucosaminyltransferase II (MGAT2), an enzyme that generates the second GlcNAcbeta1,2- branch from the trimannosyl glycan core using UDP-GlcNAc as the sugar donor. We determined the structure of human MGAT2 as a Mn(2+)-UDP donor analog complex and as a GlcNAcMan3GlcNAc2-Asn acceptor complex to reveal the structural basis for substrate recognition and catalysis. The enzyme exhibits a GT-A Rossmann-like fold that employs conserved divalent cation-dependent substrate interactions with the UDP-GlcNAc donor. MGAT2 interactions with the extended glycan acceptor are distinct from other related glycosyltransferases. These interactions are composed of a catalytic subsite that binds the Man-alpha1,6- monosaccharide acceptor and a distal exosite pocket that binds the GlcNAc-beta1,2Man-alpha1,3Manbeta- substrate "recognition arm." Recognition arm interactions are similar to the enzyme-substrate interactions for Golgi alpha-mannosidase II, a glycoside hydrolase that acts just before MGAT2 in the Asn-linked glycan biosynthetic pathway. These data suggest that substrate binding by MGAT2 employs both conserved and convergent catalytic subsite modules to provide substrate selectivity and catalysis. More broadly, the MGAT2 active-site architecture demonstrates how glycosyltransferases create complementary modular templates for regiospecific extension of glycan structures in mammalian cells.

Human N-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite.,Kadirvelraj R, Yang JY, Sanders JH, Liu L, Ramiah A, Prabhakar PK, Boons GJ, Wood ZA, Moremen KW Proc Natl Acad Sci U S A. 2018 Apr 16. pii: 1716988115. doi:, 10.1073/pnas.1716988115. PMID:29666272<ref>PMID:29666272</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vcs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kadirvelraj R]]
[[Category: Sanders JH]]
[[Category: Wood ZA]]