2yma

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<StructureSection load='2yma' size='340' side='right'caption='[[2yma]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
<StructureSection load='2yma' size='340' side='right'caption='[[2yma]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2yma]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YMA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2yma]] is a 2 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=2YMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YMA FirstGlance]. <br>
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</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=2yma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yma OCA], [https://pdbe.org/2yma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yma RCSB], [https://www.ebi.ac.uk/pdbsum/2yma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yma ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.545&#8491;</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=2yma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yma OCA], [https://pdbe.org/2yma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yma RCSB], [https://www.ebi.ac.uk/pdbsum/2yma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yma ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/OS9_YEAST OS9_YEAST]] Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific.<ref>PMID:12077121</ref> <ref>PMID:15556621</ref> <ref>PMID:16168370</ref> <ref>PMID:16168371</ref> <ref>PMID:16168372</ref>
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[https://www.uniprot.org/uniprot/OS9_YEAST OS9_YEAST] Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific.<ref>PMID:12077121</ref> <ref>PMID:15556621</ref> <ref>PMID:16168370</ref> <ref>PMID:16168371</ref> <ref>PMID:16168372</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In yeast, the membrane-bound HMG-CoA reductase degradation (HRD) ubiquitin-ligase complex is a key player of the ER-associated protein degradation pathway that targets misfolded proteins for proteolysis. Yos9, a component of the luminal submodule of the ligase, scans proteins for specific oligosaccharide modifications, which constitute a critical determinant of the degradation signal. Here, we report the crystal structure of the Yos9 domain that was previously suggested to confer binding to Hrd3, another component of the HRD complex. We observe an alphabeta-roll domain architecture and a dimeric assembly which are confirmed by analytical ultracentrifugation of both the crystallized domain and full-length Yos9. Our binding studies indicate that, instead of this domain, the N-terminal part of Yos9 including the mannose 6-phosphate receptor homology domain mediates the association with Hrd3 in vitro. Our results support the model of a dimeric state of the HRD complex and provide first-time evidence of self-association on its luminal side.
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Structural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase Complex.,Hanna J, Schutz A, Zimmermann F, Behlke J, Sommer T, Heinemann U J Biol Chem. 2012 Mar 9;287(11):8633-40. Epub 2012 Jan 18. PMID:22262864<ref>PMID:22262864</ref>
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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 2yma" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Behlke, J]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Hanna, J]]
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[[Category: Behlke J]]
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[[Category: Heinemann, U]]
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[[Category: Hanna J]]
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[[Category: Schuetz, A]]
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[[Category: Heinemann U]]
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[[Category: Sommer, T]]
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[[Category: Schuetz A]]
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[[Category: Zimmermann, F]]
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[[Category: Sommer T]]
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[[Category: Carbohydrate binding protein]]
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[[Category: Zimmermann F]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Endoplasmic reticulum-associated protein degradation]]
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[[Category: Hrd complex]]
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[[Category: Misfolded protein]]
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[[Category: Quality control]]
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Current revision

X-ray structure of the Yos9 dimerization domain

PDB ID 2yma

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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