5gpd: Difference between revisions
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<StructureSection load='5gpd' size='340' side='right'caption='[[5gpd]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='5gpd' size='340' side='right'caption='[[5gpd]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5gpd]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5gpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GPD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.501Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gpd OCA], [https://pdbe.org/5gpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gpd RCSB], [https://www.ebi.ac.uk/pdbsum/5gpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gpd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SREBP_SCHPO SREBP_SCHPO] Transcriptional activator required for transcription of genes required for adaptation to anaerobic growth like those implicated in the nonrespiratory oxygen-consumptive biosynthetic pathways of sterol, heme, sphingolipid, and ubiquinone biosynthesis. May monitor oxygen levels through sterol synthesis steps which require oxygen.<ref>PMID:15797383</ref> <ref>PMID:16537923</ref> <ref>PMID:18276645</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Schizosaccharomyces pombe 972h-]] | ||
[[Category: | [[Category: Gong X]] | ||
[[Category: | [[Category: Qian HW]] | ||
[[Category: | [[Category: Wu JP]] | ||
[[Category: | [[Category: Yan N]] | ||
Revision as of 14:38, 2 August 2023
Crystal structure of the binding domain of SREBP from fission yeastCrystal structure of the binding domain of SREBP from fission yeast
Structural highlights
FunctionSREBP_SCHPO Transcriptional activator required for transcription of genes required for adaptation to anaerobic growth like those implicated in the nonrespiratory oxygen-consumptive biosynthetic pathways of sterol, heme, sphingolipid, and ubiquinone biosynthesis. May monitor oxygen levels through sterol synthesis steps which require oxygen.[1] [2] [3] Publication Abstract from PubMedSterol regulatory element-binding protein (SREBP) transcription factors are master regulators of cellular lipid homeostasis in mammals and oxygen-responsive regulators of hypoxic adaptation in fungi. SREBP C-terminus binds to the WD40 domain of SREBP cleavage-activating protein (SCAP), which confers sterol regulation by controlling the ER-to-Golgi transport of the SREBP-SCAP complex and access to the activating proteases in the Golgi. Here, we biochemically and structurally show that the carboxyl terminal domains (CTD) of Sre1 and Scp1, the fission yeast SREBP and SCAP, form a functional 4:4 oligomer and Sre1-CTD forms a dimer of dimers. The crystal structure of Sre1-CTD at 3.5 A and cryo-EM structure of the complex at 5.4 A together with in vitro biochemical evidence elucidate three distinct regions in Sre1-CTD required for Scp1 binding, Sre1-CTD dimerization and tetrameric formation. Finally, these structurally identified domains are validated in a cellular context, demonstrating that the proper 4:4 oligomeric complex formation is required for Sre1 activation. Complex structure of the fission yeast SREBP-SCAP binding domains reveals an oligomeric organization.,Gong X, Qian H, Shao W, Li J, Wu J, Liu JJ, Li W, Wang HW, Espenshade P, Yan N Cell Res. 2016 Nov;26(11):1197-1211. doi: 10.1038/cr.2016.123. Epub 2016 Nov 4. PMID:27811944[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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