6VKL

Negative stain reconstruction of the yeast exocyst octameric complex.

6VKL の概要

• エントリーDOI: 10.2210/pdb6vkl/pdb
• EMDBエントリー: 21226 6827
• 分子名称: Exocyst complex component SEC3, Exocyst complex component SEC5, Exocyst complex component SEC6, ... (8 entities in total)
• 機能のキーワード: exocyst, coiled-coil, exocytosis
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 845691.45

構造登録者

Frost, A.,Munson, M. (登録日: 2020-01-21, 公開日: 2020-07-29, 最終更新日: 2024-03-06)

主引用文献

Rossi, G.,Lepore, D.,Kenner, L.,Czuchra, A.B.,Plooster, M.,Frost, A.,Munson, M.,Brennwald, P.
Exocyst structural changes associated with activation of tethering downstream of Rho/Cdc42 GTPases.
J. Cell Biol., 219:-, 2020

PubMed Abstract: The exocyst complex plays a critical role in determining both temporal and spatial dynamics of exocytic vesicle tethering and fusion with the plasma membrane. However, the mechanism by which the exocyst functions and how it is regulated remain poorly understood. Here we describe a novel biochemical assay for the examination of exocyst function in vesicle tethering. Importantly, the assay is stimulated by gain-of-function mutations in the Exo70 component of the exocyst, selected for their ability to bypass Rho/Cdc42 activation in vivo. Single-particle electron microscopy and 3D reconstructions of negatively stained exocyst complexes reveal a structural change in the mutant exocyst that exposes a binding site for the v-SNARE. We demonstrate a v-SNARE requirement in our tethering assay and increased v-SNARE binding to exocyst gain-of-function complexes. Together, these data suggest an allosteric mechanism for activation involving a conformational change in one subunit of the complex, which is relayed through the complex to regulate its biochemical activity in vitro, as well as overall function in vivo.

PubMed: 31904797
DOI: 10.1083/jcb.201904161

実験手法

ELECTRON MICROSCOPY (15 Å)