3g9b
From Proteopedia
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<StructureSection load='3g9b' size='340' side='right'caption='[[3g9b]], [[Resolution|resolution]] 1.96Å' scene=''> | <StructureSection load='3g9b' size='340' side='right'caption='[[3g9b]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3g9b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3g9b]] 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=3G9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G9B FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3g9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9b OCA], [https://pdbe.org/3g9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9b RCSB], [https://www.ebi.ac.uk/pdbsum/3g9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9b 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=3g9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9b OCA], [https://pdbe.org/3g9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9b RCSB], [https://www.ebi.ac.uk/pdbsum/3g9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/OST6_YEAST OST6_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. Can participate in redox reactions and is able to catalyze dithiol-disulfide exchange reactions with other proteins, albeit with relatively low efficiency. May form transient disulfide bonds with nascent polypeptides in the endoplasmic reticulum and thereby promote efficient glycosylation. 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 oligosaccharyl transferase activity.<ref>PMID:19549845</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3g9b ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3g9b ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Asparagine-linked glycosylation is a common posttranslational modification of diverse secretory and membrane proteins in eukaryotes, where it is catalyzed by the multiprotein complex oligosaccharyltransferase. The functions of the protein subunits of oligoasccharyltransferase, apart from the catalytic Stt3p, are ill defined. Here we describe functional and structural investigations of the Ost3/6p components of the yeast enzyme. Genetic, biochemical and structural analyses of the lumenal domain of Ost6p revealed oxidoreductase activity mediated by a thioredoxin-like fold with a distinctive active-site loop that changed conformation with redox state. We found that mutation of the active-site cysteine residues of Ost6p and its paralogue Ost3p affected the glycosylation efficiency of a subset of glycosylation sites. Our results show that eukaryotic oligosaccharyltransferase is a multifunctional enzyme that acts at the crossroads of protein modification and protein folding. | ||
| - | + | ==See Also== | |
| - | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
| - | [[Category: Dolichyl-diphosphooligosaccharide--protein glycotransferase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Aebi | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Brozzo | + | [[Category: Aebi M]] |
| - | [[Category: Capitani | + | [[Category: Brozzo MS]] |
| - | [[Category: Fritsch | + | [[Category: Capitani G]] |
| - | [[Category: Glockshuber | + | [[Category: Fritsch F]] |
| - | [[Category: Grimshaw | + | [[Category: Glockshuber R]] |
| - | [[Category: Gruetter | + | [[Category: Grimshaw JPA]] |
| - | [[Category: Schulz | + | [[Category: Gruetter MG]] |
| - | [[Category: Stirnimann | + | [[Category: Schulz BL]] |
| - | + | [[Category: Stirnimann CU]] | |
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Current revision
Crystal structure of reduced Ost6L
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