1LDJ

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

Summary for 1LDJ

• Entry DOI: 10.2210/pdb1ldj/pdb
• Related: 1LDD 1LDK
• Descriptor: Cullin homolog 1, ring-box protein 1, ZINC ION (3 entities in total)
• Functional Keywords: cullin, rbx1, roc1, hrt1, zinc ring finger, ligase, ubiquitin, ubiquitination, scf
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P62877
• Total number of polymer chains: 2
• Total formula weight: 98925.89

Authors

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. (deposition date: 2002-04-08, release date: 2002-05-08, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3 Å)