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| | <StructureSection load='6p28' size='340' side='right'caption='[[6p28]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='6p28' size='340' side='right'caption='[[6p28]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6p28]] 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=6P28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P28 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6p28]] 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=6P28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P28 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT2, FUN25, YAL023C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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]] 1.35Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dolichyl-phosphate-mannose--protein_mannosyltransferase Dolichyl-phosphate-mannose--protein mannosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.109 2.4.1.109] </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=6p28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p28 OCA], [https://pdbe.org/6p28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p28 RCSB], [https://www.ebi.ac.uk/pdbsum/6p28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p28 ProSAT]</span></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=6p28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p28 OCA], [http://pdbe.org/6p28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p28 RCSB], [http://www.ebi.ac.uk/pdbsum/6p28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p28 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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: Dolichyl-phosphate-mannose--protein mannosyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bai, L]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Li, H]] | + | [[Category: Bai L]] |
| - | [[Category: Complex]] | + | [[Category: Li H]] |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Transferase]]
| + | |
| 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
In eukaryotes, a nascent peptide entering the endoplasmic reticulum (ER) is scanned by two Sec61 translocon-associated large membrane machines for protein N-glycosylation and protein O-mannosylation, respectively. While the structure of the eight-protein oligosaccharyltransferase complex has been determined recently, the structures of mannosyltransferases of the PMT family, which are an integral part of ER protein homeostasis, are still unknown. Here we report cryo-EM structures of the Saccharomyces cerevisiae Pmt1-Pmt2 complex bound to a donor and an acceptor peptide at 3.2-A resolution, showing that each subunit contains 11 transmembrane helices and a lumenal beta-trefoil fold termed the MIR domain. The structures reveal the substrate recognition model and confirm an inverting mannosyl-transferring reaction mechanism by the enzyme complex. Furthermore, we found that the transmembrane domains of Pmt1 and Pmt2 share a structural fold with the catalytic subunits of oligosaccharyltransferases, confirming a previously proposed evolutionary relationship between protein O-mannosylation and protein N-glycosylation.
Structure of the eukaryotic protein O-mannosyltransferase Pmt1-Pmt2 complex.,Bai L, Kovach A, You Q, Kenny A, Li H Nat Struct Mol Biol. 2019 Jul 8. pii: 10.1038/s41594-019-0262-6. doi:, 10.1038/s41594-019-0262-6. PMID:31285605[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
- ↑ Bai L, Kovach A, You Q, Kenny A, Li H. Structure of the eukaryotic protein O-mannosyltransferase Pmt1-Pmt2 complex. Nat Struct Mol Biol. 2019 Jul 8. pii: 10.1038/s41594-019-0262-6. doi:, 10.1038/s41594-019-0262-6. PMID:31285605 doi:http://dx.doi.org/10.1038/s41594-019-0262-6
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