- EMDB-11212: Cryo-EM structure of ESCRT-III helical Vps24 filaments -
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基本情報
登録情報
データベース: EMDB / ID: EMD-11212
タイトル
Cryo-EM structure of ESCRT-III helical Vps24 filaments
マップデータ
Sharpened cryo EM density
試料
複合体: Doubled-stranded helical filament assembly of Vps24
タンパク質・ペプチド: Vacuolar protein-sorting-associated protein 24
キーワード
Filament / Helical / Membrane Remodeling / LIPID BINDING PROTEIN
機能・相同性
機能・相同性情報
Sealing of the nuclear envelope (NE) by ESCRT-III / intralumenal vesicle formation / Macroautophagy / ATP export / ESCRT III complex / Endosomal Sorting Complex Required For Transport (ESCRT) / endosome transport via multivesicular body sorting pathway / late endosome to vacuole transport / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / multivesicular body ...Sealing of the nuclear envelope (NE) by ESCRT-III / intralumenal vesicle formation / Macroautophagy / ATP export / ESCRT III complex / Endosomal Sorting Complex Required For Transport (ESCRT) / endosome transport via multivesicular body sorting pathway / late endosome to vacuole transport / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / multivesicular body / protein transport / identical protein binding / cytosol / cytoplasm 類似検索 - 分子機能
ジャーナル: Sci Adv / 年: 2020 タイトル: Structure and assembly of ESCRT-III helical Vps24 filaments. 著者: Stefan T Huber / Siavash Mostafavi / Simon A Mortensen / Carsten Sachse / 要旨: ESCRT-III proteins mediate a range of cellular membrane remodeling activities such as multivesicular body biogenesis, cytokinesis, and viral release. Critical to these processes is the assembly of ...ESCRT-III proteins mediate a range of cellular membrane remodeling activities such as multivesicular body biogenesis, cytokinesis, and viral release. Critical to these processes is the assembly of ESCRT-III subunits into polymeric structures. In this study, we determined the cryo-EM structure of a helical assembly of Vps24 at 3.2-Å resolution and found that Vps24 adopts an elongated open conformation. Vps24 forms a domain-swapped dimer extended into protofilaments that associate into a double-stranded apolar filament. We demonstrate that, upon binding negatively charged lipids, Vps24 homopolymer filaments undergo partial disassembly into shorter filament fragments and oligomers. Upon the addition of Vps24, Vps2, and Snf7, liposomes are deformed into neck and tubular structures by an ESCRT-III heteropolymer coat. The filamentous Vps24 homopolymer assembly structure and interaction studies reveal how Vps24 could introduce unique geometric properties to mixed-type ESCRT-III heteropolymers and contribute to the process of membrane scission events.
EMPIAR-10495 (タイトル: Structure and assembly of ESCRT-III helical Vps24 filaments Data size: 70.0 Data #1: Aligned micrographs of Vps24 helical filaments [micrographs - single frame])
凍結剤: ETHANE-PROPANE / チャンバー内湿度: 100 % / チャンバー内温度: 283 K / 装置: FEI VITROBOT MARK IV
詳細
Sample was concentrated to 5 mg/mL, incubated in the refridgerator overnight, ultracentrifugated, and resuspended to a final concentration of 0.9 mg/mL for cryo-EM
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電子顕微鏡法
顕微鏡
FEI TITAN KRIOS
撮影
フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 検出モード: COUNTING / デジタル化 - 画像ごとのフレーム数: 1-40 / 実像数: 3257 / 平均電子線量: 1.0 e/Å2 詳細: 1320 images were manually selected for further processing