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1U5T

Structure of the ESCRT-II endosomal trafficking complex

1U5T の概要
エントリーDOI10.2210/pdb1u5t/pdb
分子名称appears to be functionally related to SNF7; Snf8p, Defective in vacuolar protein sorting; Vps36p, Hypothetical 23.6 kDa protein in YUH1-URA8 intergenic region (3 entities in total)
機能のキーワードescrt, endosomal, trafficking, protein complex, transport protein
由来する生物種Saccharomyces cerevisiae (baker's yeast)
詳細
細胞内の位置Cytoplasm: Q12483 Q06696 P47142
タンパク質・核酸の鎖数4
化学式量合計93811.00
構造登録者
Hierro, A.,Sun, J.,Rusnak, A.S.,Kim, J.,Prag, G.,Emr, S.D.,Hurley, J.H. (登録日: 2004-07-28, 公開日: 2004-09-21, 最終更新日: 2024-02-14)
主引用文献Hierro, A.,Sun, J.,Rusnak, A.S.,Kim, J.,Prag, G.,Emr, S.D.,Hurley, J.H.
Structure of ESCRT-II endosomal trafficking complex
Nature, 431:221-225, 2004
Cited by
PubMed Abstract: The multivesicular-body (MVB) pathway delivers transmembrane proteins and lipids to the lumen of the endosome. The multivesicular-body sorting pathway has crucial roles in growth-factor-receptor downregulation, developmental signalling, regulation of the immune response and the budding of certain enveloped viruses such as human immunodeficiency virus. Ubiquitination is a signal for sorting into the MVB pathway, which also requires the functions of three protein complexes, termed ESCRT-I, -II and -III (endosomal sorting complex required for transport). Here we report the crystal structure of the core of the yeast ESCRT-II complex, which contains one molecule of the Vps protein Vps22, the carboxy-terminal domain of Vps36 and two molecules of Vps25, and has the shape of a capital letter 'Y'. The amino-terminal coiled coil of Vps22 and the flexible linker leading to the ubiquitin-binding NZF domain of Vps36 both protrude from the tip of one branch of the 'Y'. Vps22 and Vps36 form nearly equivalent interactions with the two Vps25 molecules at the centre of the 'Y'. The structure suggests how ubiquitinated cargo could be passed between ESCRT components of the MVB pathway through the sequential transfer of ubiquitinated cargo from one complex to the next.
PubMed: 15329733
DOI: 10.1038/nature02914
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.6 Å)
構造検証レポート
Validation report summary of 1u5t
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2024-11-06に公開中

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