1S1Q

TSG101(UEV) domain in complex with Ubiquitin

1S1Q の概要

• エントリーDOI: 10.2210/pdb1s1q/pdb
• 関連するPDBエントリー: 1KPP 1KPQ 1M4P 1M4Q
• 分子名称: Tumor susceptibility gene 101 protein, ubiquitin, COPPER (II) ION, ... (6 entities in total)
• 機能のキーワード: heterodimer, translation, protein turnover
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: Q99816
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51741.65

構造登録者

Sundquist, W.I.,Schubert, H.L.,Kelly, B.N.,Hill, G.C.,Holton, J.M.,Hill, C.P. (登録日: 2004-01-07, 公開日: 2004-05-04, 最終更新日: 2024-10-30)

主引用文献

Sundquist, W.I.,Schubert, H.L.,Kelly, B.N.,Hill, G.C.,Holton, J.M.,Hill, C.P.
Ubiquitin recognition by the human TSG101 protein
Mol.Cell, 13:783-789, 2004

PubMed Abstract: The UEV domain of the TSG101 protein functions in both HIV-1 budding and the vacuolar protein sorting (VPS) pathway, where it binds ubiquitylated proteins as they are sorted into vesicles that bud into late endosomal compartments called multivesicular bodies (MVBs). TSG101 UEV-ubiquitin interactions are therefore important for delivery of both substrates and hydrolytic enzymes to lysosomes, which receive proteins via fusion with MVBs. Here, we report the crystal structure of the TSG101 UEV domain in complex with ubiquitin at 2.0 A resolution. TSG101 UEV contacts the Ile44 surface and an adjacent loop of ubiquitin through a highly solvated interface. Mutations that disrupt the interface inhibit MVB sorting, and the structure also explains how the TSG101 UEV can independently bind its ubiquitin and Pro-Thr/Ser-Ala-Pro peptide ligands. Remarkably, comparison with mapping data from other UEV and related E2 proteins indicates that although the different E2/UEV domains share the same structure and have conserved ubiquitin binding activity, they bind through very different interfaces.

PubMed: 15053872
DOI: 10.1016/S1097-2765(04)00129-7

実験手法

X-RAY DIFFRACTION (2 Å)