Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Ning Zheng, Brenda A. Schulman, Langzhou Song, Julie J. Miller, Philip D. Jeffrey, Ping Wang, Claire Chu, Deanna M. Koepp, Stephen J. Elledge, Michele Pagano, Ronald C. Conaway, Joan W. Conaway, J. Wade Harper and Nikola P. Pavletich ()
Additional contact information
Ning Zheng: Memorial Sloan-Kettering Cancer Center
Brenda A. Schulman: Memorial Sloan-Kettering Cancer Center
Langzhou Song: Memorial Sloan-Kettering Cancer Center
Julie J. Miller: Memorial Sloan-Kettering Cancer Center
Philip D. Jeffrey: Memorial Sloan-Kettering Cancer Center
Ping Wang: Memorial Sloan-Kettering Cancer Center
Claire Chu: Stowers Institute for Medical Research
Deanna M. Koepp: Stowers Institute for Medical Research
Stephen J. Elledge: Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center
Michele Pagano: Baylor College of Medicine
Ronald C. Conaway: NYU Medical Center
Joan W. Conaway: NYU Medical Center
J. Wade Harper: Stowers Institute for Medical Research
Nikola P. Pavletich: Memorial Sloan-Kettering Cancer Center

Nature, 2002, vol. 416, issue 6882, 703-709

Abstract: 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 β-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 Å 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.

Date: 2002
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DOI: 10.1038/416703a

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