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| | ==Crystal structure of Saccharomyces cerevisiae Mnn9 in complex with GDP and Mn.== | | ==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=''> | + | <StructureSection load='3zf8' size='340' side='right'caption='[[3zf8]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZF8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zf8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zf8 OCA], [http://pdbe.org/3zf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zf8 RCSB], [http://www.ebi.ac.uk/pdbsum/3zf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zf8 ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [[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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Baker's yeast]] | | [[Category: Baker's yeast]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Aalten, D M.F van]] | | [[Category: Aalten, D M.F van]] |
| | [[Category: Schuettelkopf, A W]] | | [[Category: Schuettelkopf, A W]] |
| | [[Category: Striebeck, A]] | | [[Category: Striebeck, A]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| Structural highlights
Function
[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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stolz J, Munro S. The components of the Saccharomyces cerevisiae mannosyltransferase complex M-Pol I have distinct functions in mannan synthesis. J Biol Chem. 2002 Nov 22;277(47):44801-8. Epub 2002 Sep 15. PMID:12235155 doi:10.1074/jbc.M208023200
- ↑ Striebeck A, Robinson DA, Schuttelkopf AW, van Aalten DM. Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis. Open Biol. 2013 Sep 11;3(9):130022. doi: 10.1098/rsob.130022. PMID:24026536 doi:10.1098/rsob.130022
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