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| | <StructureSection load='6zqq' size='340' side='right'caption='[[6zqq]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='6zqq' size='340' side='right'caption='[[6zqq]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zqq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZQQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZQQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zqq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZQQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT3, GI526_G0005657 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqq OCA], [http://pdbe.org/6zqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zqq RCSB], [http://www.ebi.ac.uk/pdbsum/6zqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqq 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=6zqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqq OCA], [https://pdbe.org/6zqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zqq RCSB], [https://www.ebi.ac.uk/pdbsum/6zqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A6A5Q4I2_YEASX A0A6A5Q4I2_YEASX]] Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.[RuleBase:RU367007] | + | [https://www.uniprot.org/uniprot/PMT3_YEAST PMT3_YEAST] Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to have redundant activity to PMT2.<ref>PMID:9184828</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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chiapparino, A]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hackmann, Y]] | + | [[Category: Chiapparino A]] |
| - | [[Category: Mortensen, S]] | + | [[Category: Hackmann Y]] |
| - | [[Category: Sinning, I]] | + | [[Category: Mortensen S]] |
| - | [[Category: Wild, K]] | + | [[Category: Sinning I]] |
| - | [[Category: Beta-trefoil]]
| + | [[Category: Wild K]] |
| - | [[Category: Carbohydrate-binding module]]
| + | |
| - | [[Category: Mir domain]]
| + | |
| - | [[Category: Peptide binding protein]]
| + | |
| - | [[Category: Protein-o-mannosylation]]
| + | |
| Structural highlights
Function
PMT3_YEAST Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to have redundant activity to PMT2.[1]
Publication Abstract from PubMed
Protein O-mannosyltransferases (PMTs) represent a conserved family of multispanning endoplasmic reticulum membrane proteins involved in glycosylation of S/T-rich protein substrates and unfolded proteins. PMTs work as dimers and contain a luminal MIR domain with a beta-trefoil fold, which is susceptive for missense mutations causing alpha-dystroglycanopathies in humans. Here, we analyze PMT-MIR domains by an integrated structural biology approach using X-ray crystallography and NMR spectroscopy and evaluate their role in PMT function in vivo. We determine Pmt2- and Pmt3-MIR domain structures and identify two conserved mannose-binding sites, which are consistent with general beta-trefoil carbohydrate-binding sites (alpha, beta), and also a unique PMT2-subfamily exposed FKR motif. We show that conserved residues in site alpha influence enzyme processivity of the Pmt1-Pmt2 heterodimer in vivo. Integration of the data into the context of a Pmt1-Pmt2 structure and comparison with homologous beta-trefoil - carbohydrate complexes allows for a functional description of MIR domains in protein O-mannosylation.
Functional implications of MIR domains in protein O-mannosylation.,Chiapparino A, Grbavac A, Jonker HR, Hackmann Y, Mortensen S, Zatorska E, Schott A, Stier G, Saxena K, Wild K, Schwalbe H, Strahl S, Sinning I Elife. 2020 Dec 24;9. pii: 61189. doi: 10.7554/eLife.61189. PMID:33357379[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gentzsch M, Tanner W. Protein-O-glycosylation in yeast: protein-specific mannosyltransferases. Glycobiology. 1997 Jun;7(4):481-6. PMID:9184828 doi:10.1093/glycob/7.4.481
- ↑ Chiapparino A, Grbavac A, Jonker HR, Hackmann Y, Mortensen S, Zatorska E, Schott A, Stier G, Saxena K, Wild K, Schwalbe H, Strahl S, Sinning I. Functional implications of MIR domains in protein O-mannosylation. Elife. 2020 Dec 24;9. pii: 61189. doi: 10.7554/eLife.61189. PMID:33357379 doi:http://dx.doi.org/10.7554/eLife.61189
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