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| | <StructureSection load='6zqp' size='340' side='right'caption='[[6zqp]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='6zqp' size='340' side='right'caption='[[6zqp]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zqp]] is a 1 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=6ZQP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZQP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zqp]] is a 1 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=6ZQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZQP 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>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT2, GI526_G0000041 ([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>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6zqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqp OCA], [http://pdbe.org/6zqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zqp RCSB], [http://www.ebi.ac.uk/pdbsum/6zqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqp 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=6zqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqp OCA], [https://pdbe.org/6zqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zqp RCSB], [https://www.ebi.ac.uk/pdbsum/6zqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A6A5PTF1_YEASX A0A6A5PTF1_YEASX]] Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.[RuleBase:RU367007] | + | [https://www.uniprot.org/uniprot/PMT2_YEAST PMT2_YEAST] Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.<ref>PMID:15377669</ref> <ref>PMID:18182384</ref> <ref>PMID:21147851</ref> <ref>PMID:8543034</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
PMT2_YEAST Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.[1] [2] [3] [4]
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakatsukasa K, Okada S, Umebayashi K, Fukuda R, Nishikawa S, Endo T. Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast. J Biol Chem. 2004 Nov 26;279(48):49762-72. doi: 10.1074/jbc.M403234200. Epub 2004, Sep 17. PMID:15377669 doi:http://dx.doi.org/10.1074/jbc.M403234200
- ↑ Hirayama H, Fujita M, Yoko-o T, Jigami Y. O-mannosylation is required for degradation of the endoplasmic reticulum-associated degradation substrate Gas1*p via the ubiquitin/proteasome pathway in Saccharomyces cerevisiae. J Biochem. 2008 Apr;143(4):555-67. doi: 10.1093/jb/mvm249. Epub 2008 Jan 7. PMID:18182384 doi:http://dx.doi.org/10.1093/jb/mvm249
- ↑ Goder V, Melero A. Protein O-mannosyltransferases participate in ER protein quality control. J Cell Sci. 2011 Jan 1;124(Pt 1):144-53. doi: 10.1242/jcs.072181. Epub 2010 Dec, 8. PMID:21147851 doi:http://dx.doi.org/10.1242/jcs.072181
- ↑ Gentzsch M, Immervoll T, Tanner W. Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-mannosyltransferases Pmt1p and Pmt2p function as heterodimer. FEBS Lett. 1995 Dec 18;377(2):128-30. doi: 10.1016/0014-5793(95)01324-5. PMID:8543034 doi:http://dx.doi.org/10.1016/0014-5793(95)01324-5
- ↑ 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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