National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM124348
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM084210
United States
German Research Foundation (DFG)
AR1164/1-1
United States
American Heart Association
POST34030308
United States
Howard Hughes Medical Institute (HHMI)
United States
Citation
Journal: Nat Struct Mol Biol / Year: 2022 Title: Seipin forms a flexible cage at lipid droplet formation sites. Authors: Henning Arlt / Xuewu Sui / Brayden Folger / Carson Adams / Xiao Chen / Roman Remme / Fred A Hamprecht / Frank DiMaio / Maofu Liao / Joel M Goodman / Robert V Farese / Tobias C Walther / Abstract: Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, ...Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, with a yet unclear function. Here, we report a structure of S. cerevisiae seipin based on cryogenic-electron microscopy and structural modeling data. Seipin forms a decameric, cage-like structure with the lumenal domains forming a stable ring at the cage floor and transmembrane segments forming the cage sides and top. The transmembrane segments interact with adjacent monomers in two distinct, alternating conformations. These conformations result from changes in switch regions, located between the lumenal domains and the transmembrane segments, that are required for seipin function. Our data indicate a model for LD formation in which a closed seipin cage enables triacylglycerol phase separation and subsequently switches to an open conformation to allow LD growth and budding.
Conc.: 3.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: This sample was monodisperse.
Average exposure time: 1.9 sec. / Electron dose: 54.59 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 12655
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Processing
EM software
ID
Name
Version
Category
2
SerialEM
3.6
imageacquisition
11
RELION
3
finalEulerassignment
12
RELION
3
classification
13
RELION
3
3Dreconstruction
CTF correction
Type: NONE
Symmetry
Point symmetry: C5 (5 fold cyclic)
3D reconstruction
Resolution: 3.45 Å / Resolution method: FSC 0.5 CUT-OFF / Num. of particles: 49028 / Num. of class averages: 1 / Symmetry type: POINT
Atomic model building
Protocol: AB INITIO MODEL
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