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4Q66

Structure of Exomer bound to Arf1.

4Q66 の概要
エントリーDOI10.2210/pdb4q66/pdb
関連するPDBエントリー4GNS 4IN3
分子名称Chs5p, Protein BCH1, ADP-ribosylation factor 1, ... (5 entities in total)
機能のキーワードcargo adaptor, secretory vesicle, small gtp-ase arf1-binding, trans-golgi network, protein transport
由来する生物種Saccharomyces cerevisiae R008 (Baker's yeast)
詳細
細胞内の位置Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein : Q05029
Golgi apparatus: P11076
タンパク質・核酸の鎖数12
化学式量合計581631.24
構造登録者
Paczkowski, J.E.,Fromme, J.C. (登録日: 2014-04-21, 公開日: 2014-09-17, 最終更新日: 2024-02-28)
主引用文献Paczkowski, J.E.,Fromme, J.C.
Structural basis for membrane binding and remodeling by the exomer secretory vesicle cargo adaptor.
Dev.Cell, 30:610-624, 2014
Cited by
PubMed Abstract: Cargo adaptor subunits of vesicle coat protein complexes sort transmembrane proteins to distinct membrane compartments in eukaryotic cells. The exomer complex is the only cargo adaptor known to sort proteins at the trans-Golgi network into secretory vesicles. Exomer function is regulated by the Arf1 GTPase, a master regulator of trafficking at the Golgi. We report the structure of exomer bound to two copies of Arf1. Exomer interacts with each Arf1 molecule via two surfaces, one of which is a noncanonical interface that regulates GTP hydrolysis. The structure uncovers an unexpected membrane-proximal hydrophobic element that exomer uses in cooperation with Arf1 to remodel membranes. Given the constrained motion of the exomer hinge region, we envision that exomer dynamically positions multiple membrane insertion elements to drive membrane fission. In contrast to other known cargo adaptors, exomer therefore couples two functions, cargo sorting and membrane fission, into a single complex.
PubMed: 25203211
DOI: 10.1016/j.devcel.2014.07.014
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.354 Å)
構造検証レポート
Validation report summary of 4q66
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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