4BBN

NEDD4 HECT-Ub:Ub complex

4BBN の概要

• エントリーDOI: 10.2210/pdb4bbn/pdb
• 関連するPDBエントリー: 2XBB 2XBF 4BE8
• 分子名称: E3 UBIQUITIN-PROTEIN LIGASE NEDD4, POLYUBIQUITIN-B, ... (4 entities in total)
• 機能のキーワード: ligase-signaling protein complex, ligase, ubiquitination, ligase/signaling protein
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P46934 P0CG53 P0CG53
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 62830.66

構造登録者

Maspero, E.,Valentini, E.,Mari, S.,Cecatiello, V.,Polo, S.,Pasqualato, S. (登録日: 2012-09-27, 公開日: 2013-05-01, 最終更新日: 2024-11-20)

主引用文献

Maspero, E.,Valentini, E.,Mari, S.,Cecatiello, V.,Soffientini, P.,Pasqualato, S.,Polo, S.
Structure of a Ubiquitin-Loaded Hect Ligase Reveals the Molecular Basis for Catalytic Priming
Nat.Struct.Mol.Biol., 20:696-, 2013

PubMed Abstract: Homologous to E6-AP C terminus (HECT) E3 ligases recognize and directly catalyze ligation of ubiquitin (Ub) to their substrates. Molecular details of this process remain unknown. We report the first structure, to our knowledge, of a Ub-loaded E3, the human neural precursor cell-expressed developmentally downregulated protein 4 (Nedd4). The HECT(Nedd4)~Ub transitory intermediate provides a structural basis for the proposed sequential addition mechanism. The donor Ub, transferred from the E2, is bound to the Nedd4 C lobe with its C-terminal tail locked in an extended conformation, primed for catalysis. We provide evidence that the Nedd4-family members are Lys63-specific enzymes whose catalysis is mediated by an essential C-terminal acidic residue.

PubMed: 23644597
DOI: 10.1038/NSMB.2566

実験手法

X-RAY DIFFRACTION (2.51 Å)