1ldd
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Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex
OverviewOverview
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.
About this StructureAbout this Structure
1LDD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex., Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP, Nature. 2002 Apr 18;416(6882):703-9. PMID:11961546
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