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3g9b

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Revision as of 05:59, 7 December 2018

Crystal structure of reduced Ost6L

Structural highlights

3g9b is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3g7y
Gene:	OST6, YML019W (ATCC 18824)
Activity:	Dolichyl-diphosphooligosaccharide--protein glycotransferase, with EC number 2.4.99.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency.,Schulz BL, Stirnimann CU, Grimshaw JP, Brozzo MS, Fritsch F, Mohorko E, Capitani G, Glockshuber R, Grutter MG, Aebi M Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11061-6. Epub 2009 Jun 23. PMID:19549845^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schulz BL, Stirnimann CU, Grimshaw JP, Brozzo MS, Fritsch F, Mohorko E, Capitani G, Glockshuber R, Grutter MG, Aebi M. Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency. Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11061-6. Epub 2009 Jun 23. PMID:19549845
↑ Schulz BL, Stirnimann CU, Grimshaw JP, Brozzo MS, Fritsch F, Mohorko E, Capitani G, Glockshuber R, Grutter MG, Aebi M. Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency. Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11061-6. Epub 2009 Jun 23. PMID:19549845

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3g9b"

@@ Line 1: / Line 1: @@
 ==Crystal structure of reduced Ost6L==
 <StructureSection load='3g9b' size='340' side='right' caption='[[3g9b]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OST6, YML019W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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='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=3g9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9b OCA], [http://pdbe.org/3g9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g9b RCSB], [http://www.ebi.ac.uk/pdbsum/3g9b PDBsum]</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=3g9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9b OCA], [http://pdbe.org/3g9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g9b RCSB], [http://www.ebi.ac.uk/pdbsum/3g9b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9b ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g9/3g9b_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g9/3g9b_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3g9b

From Proteopedia

Revision as of 05:59, 7 December 2018

Crystal structure of reduced Ost6L

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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