This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7oxr
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of yeast Sei1 with locking helix deletion== | |
| + | <StructureSection load='7oxr' size='340' side='right'caption='[[7oxr]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7oxr]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OXR FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7oxp|7oxp]]</div></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=7oxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oxr OCA], [https://pdbe.org/7oxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oxr RCSB], [https://www.ebi.ac.uk/pdbsum/7oxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oxr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lipid droplets (LDs) are universal lipid storage organelles with a core of neutral lipids, such as triacylglycerols, surrounded by a phospholipid monolayer. This unique architecture is generated during LD biogenesis at endoplasmic reticulum (ER) sites marked by Seipin, a conserved membrane protein mutated in lipodystrophy. Here structural, biochemical and molecular dynamics simulation approaches reveal the mechanism of LD formation by the yeast Seipin Sei1 and its membrane partner Ldb16. We show that Sei1 luminal domain assembles a homooligomeric ring, which, in contrast to other Seipins, is unable to concentrate triacylglycerol. Instead, Sei1 positions Ldb16, which concentrates triacylglycerol within the Sei1 ring through critical hydroxyl residues. Triacylglycerol recruitment to the complex is further promoted by Sei1 transmembrane segments, which also control Ldb16 stability. Thus, we propose that LD assembly by the Sei1/Ldb16 complex, and likely other Seipins, requires sequential triacylglycerol-concentrating steps via distinct elements in the ER membrane and lumen. | ||
| - | + | Mechanism of lipid droplet formation by the yeast Sei1/Ldb16 Seipin complex.,Klug YA, Deme JC, Corey RA, Renne MF, Stansfeld PJ, Lea SM, Carvalho P Nat Commun. 2021 Oct 8;12(1):5892. doi: 10.1038/s41467-021-26162-6. PMID:34625558<ref>PMID:34625558</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7oxr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Deme, J C]] | ||
| + | [[Category: Lea, S M]] | ||
| + | [[Category: Lipid binding]] | ||
| + | [[Category: Lipid droplet formation]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Seipin]] | ||
Current revision
Cryo-EM structure of yeast Sei1 with locking helix deletion
| |||||||||||
