7oxr | pdb_00007oxr

Cryo-EM structure of yeast Sei1 with locking helix deletion

spinqualitylabelsall models 7oxr, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7oxr is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 7oxp Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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