3zf8: Difference between revisions
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==Crystal structure of Saccharomyces cerevisiae Mnn9 in complex with GDP and Mn.== | |||
<StructureSection load='3zf8' size='340' side='right'caption='[[3zf8]], [[Resolution|resolution]] 1.98Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zf8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZF8 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]] 1.98Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <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=3zf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zf8 OCA], [https://pdbe.org/3zf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zf8 RCSB], [https://www.ebi.ac.uk/pdbsum/3zf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zf8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MNN9_YEAST MNN9_YEAST] The M-Pol I and M-Pol II complexes possess alpha-1,6-mannosyltransferase activity and are probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins. May also provide alpha-1,2-mannosyltransferase activity to the M-Pol I complex.<ref>PMID:12235155</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The fungal cell possesses an essential carbohydrate cell wall. The outer layer, mannan, is formed by mannoproteins carrying highly mannosylated O- and N-linked glycans. Yeast mannan biosynthesis is initiated by a Golgi-located complex (M-Pol I) of two GT-62 mannosyltransferases, Mnn9p and Van1p, that are conserved in fungal pathogens. Saccharomyces cerevisiae and Candida albicans mnn9 knockouts show an aberrant cell wall and increased antibiotic sensitivity, suggesting the enzyme is a potential drug target. Here, we present the structure of ScMnn9 in complex with GDP and Mn(2+), defining the fold and catalytic machinery of the GT-62 family. Compared with distantly related GT-78/GT-15 enzymes, ScMnn9 carries an unusual extension. Using a novel enzyme assay and site-directed mutagenesis, we identify conserved amino acids essential for ScMnn9 'priming' alpha-1,6-mannosyltransferase activity. Strikingly, both the presence of the ScMnn9 protein and its product, but not ScMnn9 catalytic activity, are required to activate subsequent ScVan1 processive alpha-1,6-mannosyltransferase activity in the M-Pol I complex. These results reveal the molecular basis of mannan synthesis and will aid development of inhibitors targeting this process. | |||
Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis.,Striebeck A, Robinson DA, Schuttelkopf AW, van Aalten DM Open Biol. 2013 Sep 11;3(9):130022. doi: 10.1098/rsob.130022. PMID:24026536<ref>PMID:24026536</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zf8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Schuettelkopf AW]] | |||
[[Category: Striebeck A]] | |||
[[Category: Van Aalten DMF]] | |||
