3BQ3

Crystal structure of S. cerevisiae Dcn1

3BQ3 の概要

• エントリーDOI: 10.2210/pdb3bq3/pdb
• 分子名称: Defective in cullin neddylation protein 1, GLYCEROL (3 entities in total)
• 機能のキーワード: ubiquitin, nedd8, neddylation, ubiquitination, scf, cullin, e3 ligases, e2, cell cycle, protein degradation, ligase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32589.18

構造登録者

Chou, Y.C.,Sicheri, F. (登録日: 2007-12-19, 公開日: 2008-01-29, 最終更新日: 2024-11-20)

主引用文献

Kurz, T.,Chou, Y.C.,Willems, A.R.,Meyer-Schaller, N.,Hecht, M.L.,Tyers, M.,Peter, M.,Sicheri, F.
Dcn1 Functions as a Scaffold-Type E3 Ligase for Cullin Neddylation.
Mol.Cell, 29:23-35, 2008

PubMed Abstract: Cullin-based E3 ubiquitin ligases are activated through modification of the cullin subunit with the ubiquitin-like protein Nedd8. Dcn1 regulates cullin neddylation and thus ubiquitin ligase activity. Here we describe the 1.9 A X-ray crystal structure of yeast Dcn1 encompassing an N-terminal ubiquitin-binding (UBA) domain and a C-terminal domain of unique architecture, which we termed PONY domain. A conserved surface on Dcn1 is required for direct binding to cullins and for neddylation. The reciprocal binding site for Dcn1 on Cdc53 is located approximately 18 A from the site of neddylation. Dcn1 does not require cysteine residues for catalytic function, and directly interacts with the Nedd8 E2 Ubc12 on a surface that overlaps with the E1-binding site. We show that Dcn1 is necessary and sufficient for cullin neddylation in a purified recombinant system. Taken together, these data demonstrate that Dcn1 is a scaffold-like E3 ligase for cullin neddylation.

PubMed: 18206966
DOI: 10.1016/j.molcel.2007.12.012

実験手法

X-RAY DIFFRACTION (1.9 Å)