8aff: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[8aff]] is a 12 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=8AFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AFF FirstGlance]. <br>
-</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=8aff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aff OCA], [https://pdbe.org/8aff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aff RCSB], [https://www.ebi.ac.uk/pdbsum/8aff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aff ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.87&#8491;</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=8aff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aff OCA], [https://pdbe.org/8aff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aff RCSB], [https://www.ebi.ac.uk/pdbsum/8aff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aff ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/FAT2_YEAST FAT2_YEAST] Catalyzes the first step in a degradation pathway of oxalate to CO(2) to protect the cell against the harmful effects of oxalate derived from endogenous processes or an environmental sources.<ref>PMID:24291261</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Oxalyl-CoA synthetase from Saccharomyces cerevisiae is one of the most abundant peroxisomal proteins in yeast and hence has become a model to study peroxisomal translocation. It contains a C-terminal Peroxisome Targeting Signal 1, which however is partly dispensable, suggesting additional receptor bindings sites. To unravel any additional features that may contribute to its capacity to be recognized as peroxisomal target, we determined its assembly and overall architecture by an integrated structural biology approach, including X-ray crystallography, single particle cryo-electron microscopy and small angle X-ray scattering. Surprisingly, it assembles into mixture of concentration-dependent dimers, tetramers and hexamers by dimer self-association. Hexameric particles form an unprecedented asymmetric horseshoe-like arrangement, which considerably differs from symmetric hexameric assembly found in many other protein structures. A single mutation within the self-association interface is sufficient to abolish any higher-level oligomerization, resulting in a homogenous dimeric assembly. The small C-terminal domain of yeast Oxalyl-CoA synthetase is connected by a partly flexible hinge with the large N-terminal domain, which provides the sole basis for oligomeric assembly. Our data provide a basis to mechanistically study peroxisomal translocation of this target.
-Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase.,Burgi J, Lill P, Giannopoulou EA, Jeffries CM, Chojnowski G, Raunser S, Gatsogiannis C, Wilmanns M Biol Chem. 2023 Jan 26. doi: 10.1515/hsz-2022-0273. PMID:36694962<ref>PMID:36694962</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 8aff" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>