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- Title
Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.
- Authors
Zheng, Ning; Schulman, Brenda A; Song, Langzhou; Miller, Julie J; Jeffrey, Philip D; Wang, Ping; Chu, Claire; Koepp, Deanna M; Elledge, Stephen J; Pagano, Michele; Conaway, Ronald C; Conaway, Joan W; Harper, J Wade; Pavletich, Nikola P
- 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.
- Publication
Nature, 2002, Vol 416, Issue 6882, p703
- ISSN
0028-0836
- Publication type
Journal Article
- DOI
10.1038/416703a