|
|
| (4 intermediate revisions by the same user not shown) |
| Line 1: |
Line 1: |
|
| |
|
| ==The Cryo-EM structure of a eukaryotic oligosaccharyl transferase complex== | | ==The Cryo-EM structure of a eukaryotic oligosaccharyl transferase complex== |
| <StructureSection load='6c26' size='340' side='right' caption='[[6c26]], [[Resolution|resolution]] 3.50Å' scene=''> | | <SX load='6c26' size='340' side='right' viewer='molstar' caption='[[6c26]], [[Resolution|resolution]] 3.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6c26]] is a 8 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=6C26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C26 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6c26]] is a 8 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=6C26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C26 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EGY:(4R,7R)-4-hydroxy-N,N,N-trimethyl-4,9-dioxo-7-[(undecanoyloxy)methyl]-3,5,8-trioxa-4lambda~5~-phosphadocosan-1-aminium'>EGY</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dolichyl-diphosphooligosaccharide--protein_glycotransferase Dolichyl-diphosphooligosaccharide--protein glycotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.18 2.4.99.18] </span></td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EGY:trimethyl-[2-[oxidanyl-[(2~{R})-2-tetradecanoyloxy-3-undecanoyloxy-propoxy]phosphoryl]oxyethyl]azanium'>EGY</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6c26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c26 OCA], [http://pdbe.org/6c26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c26 RCSB], [http://www.ebi.ac.uk/pdbsum/6c26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c26 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=6c26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c26 OCA], [https://pdbe.org/6c26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c26 RCSB], [https://www.ebi.ac.uk/pdbsum/6c26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c26 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/OST3_YEAST OST3_YEAST]] Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. [[http://www.uniprot.org/uniprot/OST5_YEAST OST5_YEAST]] Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. [[http://www.uniprot.org/uniprot/OSTD_YEAST OSTD_YEAST]] Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. [[http://www.uniprot.org/uniprot/OST1_YEAST OST1_YEAST]] Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. [[http://www.uniprot.org/uniprot/OSTB_YEAST OSTB_YEAST]] Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. [[http://www.uniprot.org/uniprot/STT3_YEAST STT3_YEAST]] Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.<ref>PMID:12359722</ref> [[http://www.uniprot.org/uniprot/OST4_YEAST OST4_YEAST]] Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. OST4 is required for recruitment of OST3 or OST6 to the OST complex. It is essential for cell growth at 37 but not at 25 degrees Celsius. [[http://www.uniprot.org/uniprot/OST2_YEAST OST2_YEAST]] Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. | | [https://www.uniprot.org/uniprot/STT3_YEAST STT3_YEAST] Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.<ref>PMID:12359722</ref> |
| | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == |
| | N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction is catalysed by an eight-protein oligosaccharyltransferase complex, OST, embedded in the ER membrane. Our understanding of eukaryotic protein N-glycosylation has been limited owing to the lack of high-resolution structures. Here we report a 3.5-A resolution cryo-EM structure of the Saccharomyces cerevisiae OST, revealing the structures of Ost1-5, Stt3, Wbp1, and Swp1. We found that seven phospholipids mediate many of the inter-subunit interactions, and an Stt3 N-glycan mediates interactions with Wbp1 and Swp1 in the lumen. Ost3 was found to mediate the OST-Sec61 translocon interface, funnelling the acceptor peptide towards the OST catalytic site as the nascent peptide emerges from the translocon. The structure provides novel insights into co-translational protein N-glycosylation and may facilitate the development of small-molecule inhibitors targeting this process. |
| | |
| | The atomic structure of a eukaryotic oligosaccharyltransferase complex.,Bai L, Wang T, Zhao G, Kovach A, Li H Nature. 2018 Jan 22. pii: nature25755. doi: 10.1038/nature25755. PMID:29466327<ref>PMID:29466327</ref> |
| | |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> |
| | <div class="pdbe-citations 6c26" style="background-color:#fffaf0;"></div> |
| | |
| | ==See Also== |
| | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </SX> |
| [[Category: Baker's yeast]] | | [[Category: Large Structures]] |
| [[Category: Dolichyl-diphosphooligosaccharide--protein glycotransferase]] | | [[Category: Saccharomyces cerevisiae S288C]] |
| [[Category: Bai, L]] | | [[Category: Bai L]] |
| [[Category: Li, H]] | | [[Category: Li H]] |
| [[Category: Complex]]
| |
| [[Category: Glycosylation]]
| |
| [[Category: Transferase]]
| |