2XBB

Nedd4 HECT:Ub complex

2XBB の概要

• エントリーDOI: 10.2210/pdb2xbb/pdb
• 関連するPDBエントリー: 2XBF
• 分子名称: E3 UBIQUITIN-PROTEIN LIGASE NEDD4, UBIQUITIN, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: ligase-protein binding complex, ligase/protein binding
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P46934 P0CG53
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 108902.07

構造登録者

Maspero, E.,Cecatiello, V.,Musacchio, A.,Polo, S.,Pasqualato, S. (登録日: 2010-04-08, 公開日: 2011-03-23, 最終更新日: 2023-12-20)

主引用文献

Maspero, E.,Mari, S.,Valentini, E.,Musacchio, A.,Fish, A.,Pasqualato, S.,Polo, S.
Structure of the Hect:Ubiquitin Complex and its Role in Ubiquitin Chain Elongation
Embo Rep., 12:342-, 2011

PubMed Abstract: Several mechanisms have been proposed for the synthesis of substrate-linked ubiquitin chains. HECT ligases directly catalyse protein ubiquitination and have been found to non-covalently interact with ubiquitin. We report crystal structures of the Nedd4 HECT domain, alone and in complex with ubiquitin, which show a new binding mode involving two surfaces on ubiquitin and both subdomains of the HECT N-lobe. The structures suggest a model for HECT-to-substrate ubiquitin transfer, in which the growing chain on the substrate is kept close to the catalytic cysteine to promote processivity. Mutational analysis highlights differences between the processes of substrate polyubiquitination and self-ubiquitination.

PubMed: 21399620
DOI: 10.1038/EMBOR.2011.21

実験手法

X-RAY DIFFRACTION (2.68 Å)