4ic4: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4ic4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IC4 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=4ic4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ic4 OCA], [https://pdbe.org/4ic4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ic4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ic4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ic4 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]] 1.5&#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=4ic4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ic4 OCA], [https://pdbe.org/4ic4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ic4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ic4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ic4 ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/OSH3_YEAST OSH3_YEAST]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The oxysterol-binding protein (OSBP)-related proteins (ORPs) are conserved from yeast to humans, and implicated in the regulation of lipid homeostasis and in signaling pathways. Saccharomyces cerevisiae has seven ORPs (Osh1-Osh7) that share one unknown essential function. Here, we report the 1.5-2.3 A structures of the PH domain and ORD (OSBP-related domain) of yeast Osh3 in apo-form or in complex with phosphatidylinositol 4-phosphate (PI[4]P). Osh3 recognizes PI(4)P by the highly conserved residues in the tunnel of ORD whereas it lacks sterol binding due to the narrow hydrophobic tunnel. Yeast complementation tests suggest that PI(4)P binding to PH and ORD is essential for function. This study suggests that the unifying feature in all ORP homologs is the binding of PI(4)P to ORD and sterol binding is additional to certain homologs. Structural modeling of full-length Osh3 is consistent with the concept that Osh3 is a lipid transfer protein or regulator in membrane contact sites.
-Structure of osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins.,Tong J, Yang H, Yang H, Eom SH, Im YJ Structure. 2013 Jul 2;21(7):1203-13. doi: 10.1016/j.str.2013.05.007. Epub 2013, Jun 20. PMID:23791945<ref>PMID:23791945</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ic4" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Oxysterol-binding protein homolog|Oxysterol-binding protein homolog]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>