1LDK

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex

1LDK の概要

• エントリーDOI: 10.2210/pdb1ldk/pdb
• 関連するPDBエントリー: 1LDD 1LDJ
• 分子名称: CULLIN HOMOLOG, ring-box protein 1, CYCLIN A/CDK2-ASSOCIATED PROTEIN P19, ... (6 entities in total)
• 機能のキーワード: scf, cullin, rbx1, roc1, hrt1, skp1, skp2, f-box, fbox, ubiquitin, ubiquitination, e3 ligase, ligase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 118906.87

構造登録者

Zheng, N.,Schulman, B.A.,Song, L.,Miller, J.J.,Jeffrey, P.D.,Wang, P.,Chu, C.,Koepp, D.M.,Elledge, S.J.,Pagano, M.,Conaway, R.C.,Conaway, J.W.,Harper, J.W.,Pavletich, N.P. (登録日: 2002-04-08, 公開日: 2002-05-08, 最終更新日: 2024-11-20)

主引用文献

Zheng, N.,Schulman, B.A.,Song, L.,Miller, J.J.,Jeffrey, P.D.,Wang, P.,Chu, C.,Koepp, D.M.,Elledge, S.J.,Pagano, M.,Conaway, R.C.,Conaway, J.W.,Harper, J.W.,Pavletich, N.P.
Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.
Nature, 416:703-709, 2002

PubMed Abstract: SCF complexes are the largest family of E3 ubiquitin-protein ligases and mediate the ubiquitination of diverse regulatory and signalling proteins. Here we present the crystal structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF complex, which shows that Cul1 is an elongated protein that consists of a long stalk and a globular domain. The globular domain binds the RING finger protein Rbx1 through an intermolecular beta-sheet, forming a two-subunit catalytic core that recruits the ubiquitin-conjugating enzyme. The long stalk, which consists of three repeats of a novel five-helix motif, binds the Skp1-F boxSkp2 protein substrate-recognition complex at its tip. Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart. The structure suggests that Cul1 may contribute to catalysis through the positioning of the substrate and the ubiquitin-conjugating enzyme, and this model is supported by Cul1 mutations designed to eliminate the rigidity of the scaffold.

PubMed: 11961546
DOI: 10.1038/416703a

実験手法

X-RAY DIFFRACTION (3.1 Å)