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| - | [[Image:2yma.png|left|200px]] | |
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| - | <!--
| + | ==X-ray structure of the Yos9 dimerization domain== |
| - | The line below this paragraph, containing "STRUCTURE_2yma", creates the "Structure Box" on the page.
| + | <StructureSection load='2yma' size='340' side='right'caption='[[2yma]], [[Resolution|resolution]] 2.54Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <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> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.545Å</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> |
| - | {{STRUCTURE_2yma| PDB=2yma | SCENE= }}
| + | </table> |
| - | | + | == Function == |
| - | ===X-ray structure of the Yos9 dimerization domain===
| + | [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> |
| - | | + | == References == |
| - | | + | <references/> |
| - | <!-- | + | __TOC__ |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_22262864}}, adds the Publication Abstract to the page
| + | </StructureSection> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 22262864 is the PubMed ID number.
| + | [[Category: Large Structures]] |
| - | -->
| + | |
| - | {{ABSTRACT_PUBMED_22262864}}
| + | |
| - | | + | |
| - | ==About this Structure== | + | |
| - | [[2yma]] is a 2 chain structure with sequence from [http://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]. | + | |
| - | | + | |
| - | ==Reference== | + | |
| - | <ref group="xtra">PMID:022262864</ref><references group="xtra"/> | + | |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Behlke, J.]] | + | [[Category: Behlke J]] |
| - | [[Category: Hanna, J.]] | + | [[Category: Hanna J]] |
| - | [[Category: Heinemann, U.]] | + | [[Category: Heinemann U]] |
| - | [[Category: Schuetz, A.]] | + | [[Category: Schuetz A]] |
| - | [[Category: Sommer, T.]] | + | [[Category: Sommer T]] |
| - | [[Category: Zimmermann, F.]] | + | [[Category: Zimmermann F]] |
| - | [[Category: Carbohydrate binding protein]]
| + | |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Endoplasmic reticulum-associated protein degradation]]
| + | |
| - | [[Category: Hrd complex]]
| + | |
| - | [[Category: Misfolded protein]]
| + | |
| - | [[Category: Quality control]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5]
References
- ↑ Friedmann E, Salzberg Y, Weinberger A, Shaltiel S, Gerst JE. YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins. J Biol Chem. 2002 Sep 20;277(38):35274-81. Epub 2002 Jun 20. PMID:12077121 doi:http://dx.doi.org/10.1074/jbc.M201044200
- ↑ Buschhorn BA, Kostova Z, Medicherla B, Wolf DH. A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett. 2004 Nov 19;577(3):422-6. PMID:15556621 doi:http://dx.doi.org/S0014579304012773
- ↑ Bhamidipati A, Denic V, Quan EM, Weissman JS. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol Cell. 2005 Sep 16;19(6):741-51. PMID:16168370 doi:http://dx.doi.org/S1097-2765(05)01524-8
- ↑ Kim W, Spear ED, Ng DT. Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell. 2005 Sep 16;19(6):753-64. PMID:16168371 doi:http://dx.doi.org/S1097-2765(05)01528-5
- ↑ Szathmary R, Bielmann R, Nita-Lazar M, Burda P, Jakob CA. Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell. 2005 Sep 16;19(6):765-75. PMID:16168372 doi:http://dx.doi.org/S1097-2765(05)01557-1
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