3JC1

Electron cryo-microscopy of the IST1-CHMP1B ESCRT-III copolymer

これはPDB形式変換不可エントリーです。

3JC1 の概要

• エントリーDOI: 10.2210/pdb3jc1/pdb
• EMDBエントリー: 6461
• 分子名称: Increased Sodium Tolerance 1 (IST1), Charged multivesicular body protein 1b (2 entities in total)
• 機能のキーワード: escrt-iii, ist1, chmp1b, membrane tubulation, helical filament, lipid binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 68
• 化学式量合計: 1321655.92

構造登録者

McCullough, J.,Clippinger, A.K.,Talledge, N.,Skowyra, M.L.,Saunders, M.G.,Naismith, T.V.,Colf, L.A.,Afonine, P.,Arthur, C.,Sundquist, W.I.,Hanson, P.I.,Frost, A. (登録日: 2015-11-09, 公開日: 2015-12-16, 最終更新日: 2024-02-21)

主引用文献

McCullough, J.,Clippinger, A.K.,Talledge, N.,Skowyra, M.L.,Saunders, M.G.,Naismith, T.V.,Colf, L.A.,Afonine, P.,Arthur, C.,Sundquist, W.I.,Hanson, P.I.,Frost, A.
Structure and membrane remodeling activity of ESCRT-III helical polymers.
Science, 350:1548-1551, 2015

PubMed Abstract: The endosomal sorting complexes required for transport (ESCRT) proteins mediate fundamental membrane remodeling events that require stabilizing negative membrane curvature. These include endosomal intralumenal vesicle formation, HIV budding, nuclear envelope closure, and cytokinetic abscission. ESCRT-III subunits perform key roles in these processes by changing conformation and polymerizing into membrane-remodeling filaments. Here, we report the 4 angstrom resolution cryogenic electron microscopy reconstruction of a one-start, double-stranded helical copolymer composed of two different human ESCRT-III subunits, charged multivesicular body protein 1B (CHMP1B) and increased sodium tolerance 1 (IST1). The inner strand comprises "open" CHMP1B subunits that interlock in an elaborate domain-swapped architecture and is encircled by an outer strand of "closed" IST1 subunits. Unlike other ESCRT-III proteins, CHMP1B and IST1 polymers form external coats on positively curved membranes in vitro and in vivo. Our analysis suggests how common ESCRT-III filament architectures could stabilize different degrees and directions of membrane curvature.

PubMed: 26634441
DOI: 10.1126/science.aad8305

実験手法

ELECTRON MICROSCOPY (4 Å)