1Y8X

Structural basis for recruitment of Ubc12 by an E2-binding domain in NEDD8's E1

1Y8X の概要

• エントリーDOI: 10.2210/pdb1y8x/pdb
• 分子名称: Ubiquitin-conjugating enzyme E2 M, Ubiquitin-activating enzyme E1C (3 entities in total)
• 機能のキーワード: ubiquitin-conjugating enzyme e2 m, ligase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29342.59

構造登録者

Huang, D.T.,Paydar, A.,Zhuang, M.,Waddell, M.B.,Holton, J.M.,Schulman, B.A. (登録日: 2004-12-13, 公開日: 2005-02-08, 最終更新日: 2024-11-06)

主引用文献

Huang, D.T.,Paydar, A.,Zhuang, M.,Waddell, M.B.,Holton, J.M.,Schulman, B.A.
Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1.
Mol.Cell, 17:341-350, 2005

PubMed Abstract: E2 conjugating enzymes play a central role in ubiquitin and ubiquitin-like protein (ublp) transfer cascades: the E2 accepts the ublp from the E1 enzyme and then the E2 often interacts with an E3 enzyme to promote ublp transfer to the target. We report here the crystal structure of a complex between the C-terminal domain from NEDD8's heterodimeric E1 (APPBP1-UBA3) and the catalytic core domain of NEDD8's E2 (Ubc12). The structure and associated mutational analyses reveal molecular details of Ubc12 recruitment by NEDD8's E1. Interestingly, the E1's Ubc12 binding domain resembles ubiquitin and recruits Ubc12 in a manner mimicking ubiquitin's interactions with ubiquitin binding domains. Structural comparison with E2-E3 complexes indicates that the E1 and E3 binding sites on Ubc12 may overlap and raises the possibility that crosstalk between E1 and E3 interacting with an E2 could influence the specificity and processivity of ublp transfer.

PubMed: 15694336
DOI: 10.1016/j.molcel.2004.12.020

実験手法

X-RAY DIFFRACTION (2.4 Å)