5FD9

X-ray Crystal Structure of ESCRT-III Snf7 core domain (conformation B)

5FD9 の概要

• エントリーDOI: 10.2210/pdb5fd9/pdb
• 関連するPDBエントリー: 5FD7
• 分子名称: Vacuolar-sorting protein SNF7 (2 entities in total)
• 機能のキーワード: escrt, snf7, active, core, protein transport
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15803.13

構造登録者

Tang, S.,Henne, W.M.,Borbat, P.P.,Buchkovich, N.J.,Freed, J.H.,Mao, Y.,Fromme, J.C.,Emr, S.D. (登録日: 2015-12-15, 公開日: 2015-12-30, 最終更新日: 2023-09-27)

主引用文献

Tang, S.,Henne, W.M.,Borbat, P.P.,Buchkovich, N.J.,Freed, J.H.,Mao, Y.,Fromme, J.C.,Emr, S.D.
Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments.
Elife, 4:-, 2015

PubMed Abstract: The endosomal sorting complexes required for transport (ESCRTs) constitute hetero-oligomeric machines that catalyze multiple topologically similar membrane-remodeling processes. Although ESCRT-III subunits polymerize into spirals, how individual ESCRT-III subunits are activated and assembled together into a membrane-deforming filament remains unknown. Here, we determine X-ray crystal structures of the most abundant ESCRT-III subunit Snf7 in its active conformation. Using pulsed dipolar electron spin resonance spectroscopy (PDS), we show that Snf7 activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces. This promotes the assembly of Snf7 arrays with ~30 Å periodicity into a membrane-sculpting filament. Using a combination of biochemical and genetic approaches, both in vitro and in vivo, we demonstrate that mutations on these protein interfaces halt Snf7 assembly and block ESCRT function. The architecture of the activated and membrane-bound Snf7 polymer provides crucial insights into the spatially unique ESCRT-III-mediated membrane remodeling.

PubMed: 26670543
DOI: 10.7554/eLife.12548

実験手法

X-RAY DIFFRACTION (1.6 Å)