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2lgz

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'''Unreleased structure'''
 
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The entry 2lgz is ON HOLD until Aug 03 2013
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==Solution structure of STT3P==
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<StructureSection load='2lgz' size='340' side='right'caption='[[2lgz]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2lgz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LGZ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgz OCA], [https://pdbe.org/2lgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lgz RCSB], [https://www.ebi.ac.uk/pdbsum/2lgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Huang, C., Bhaskaran, R., Mohanty, S.
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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<ref>PMID:22865878</ref>
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Description: Solution structure of STT3P
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2lgz" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Bhaskaran R]]
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[[Category: Huang C]]
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[[Category: Mohanty S]]

Current revision

Solution structure of STT3P

PDB ID 2lgz

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