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2lgz

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Revision as of 19:59, 1 August 2018

Solution structure of STT3P

Structural highlights

2lgz is a 1 chain structure with sequence from Baker's yeast. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	STT3, YGL022W (Baker's yeast)
Activity:	Dolichyl-diphosphooligosaccharide--protein glycotransferase, with EC number 2.4.99.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

Publication Abstract from PubMed

N-Glycosylation is an essential and highly conserved protein modification. In eukaryotes, it is catalyzed by a multisubunit membrane-associated enzyme, oligosaccharyltransferase (OT). We report the high resolution structure of the C-terminal domain of eukaryotic Stt3p. Unlike its soluble beta-sheet-rich prokaryotic counterparts, our model reveals that the C-terminal domain of yeast Stt3p is highly helical and has an overall oblate spheroid-shaped structure containing a membrane-embedded region. Anchoring of this protein segment to the endoplasmic reticulum membrane is likely to bring the membrane-embedded donor substrate closer, thus facilitating glycosylation efficiency. Structural comparison of the region near the WWDYG signature motif revealed that the acceptor substrate-binding site of yeast OT strikingly resembles its prokaryotic counterparts, suggesting a conserved mechanism of N-glycosylation from prokaryotes to eukaryotes. Furthermore, comparison of the NMR and cryo-EM structures of yeast OT revealed that the molecular architecture of this acceptor substrate-recognizing domain has interesting spatial specificity for interactions with other essential OT subunits.

Eukaryotic N-Glycosylation Occurs via the Membrane-anchored C-terminal Domain of the Stt3p Subunit of Oligosaccharyltransferase.,Huang C, Bhaskaran R, Mohanty S J Biol Chem. 2012 Sep 21;287(39):32450-8. Epub 2012 Aug 3. PMID:22865878^[2]

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

References

↑ Yan Q, Lennarz WJ. Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process. J Biol Chem. 2002 Dec 6;277(49):47692-700. Epub 2002 Sep 30. PMID:12359722 doi:http://dx.doi.org/10.1074/jbc.M208136200
↑ Huang C, Bhaskaran R, Mohanty S. Eukaryotic N-Glycosylation Occurs via the Membrane-anchored C-terminal Domain of the Stt3p Subunit of Oligosaccharyltransferase. J Biol Chem. 2012 Sep 21;287(39):32450-8. Epub 2012 Aug 3. PMID:22865878 doi:http://dx.doi.org/10.1074/jbc.M112.342253

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2lgz"

@@ Line 1: / Line 1: @@
 ==Solution structure of STT3P==
 <StructureSection load='2lgz' size='340' side='right' caption='[[2lgz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STT3, YGL022W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=2lgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgz OCA], [http://pdbe.org/2lgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lgz RCSB], [http://www.ebi.ac.uk/pdbsum/2lgz 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=2lgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgz OCA], [http://pdbe.org/2lgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lgz RCSB], [http://www.ebi.ac.uk/pdbsum/2lgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgz ProSAT]</span></td></tr>
 </table>
 == Function ==

2lgz

From Proteopedia

Revision as of 19:59, 1 August 2018

Solution structure of STT3P

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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