1U6G

Crystal Structure of The Cand1-Cul1-Roc1 Complex

Summary for 1U6G

• Entry DOI: 10.2210/pdb1u6g/pdb
• Descriptor: Cullin homolog 1, RING-box protein 1, TIP120 protein, ... (5 entities in total)
• Functional Keywords: cullin repeat, heat repeat, ring finger, ligase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P62877; Nucleus (By similarity): Q86VP6
• Total number of polymer chains: 3
• Total formula weight: 238815.87

Authors

Goldenberg, S.J.,Shumway, S.D.,Cascio, T.C.,Garbutt, K.C.,Liu, J.,Xiong, Y.,Zheng, N. (deposition date: 2004-07-29, release date: 2004-12-14, Last modification date: 2024-11-20)

Primary citation

Goldenberg, S.J.,Cascio, T.C.,Shumway, S.D.,Garbutt, K.C.,Liu, J.,Xiong, Y.,Zheng, N.
Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases
Cell(Cambridge,Mass.), 119:517-528, 2004

PubMed Abstract: The SCF ubiquitin ligase complex regulates diverse cellular functions by ubiquitinating numerous protein substrates. Cand1, a 120 kDa HEAT repeat protein, forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 complex. The crystal structure of the Cand1-Cul1-Roc1 complex shows that Cand1 adopts a highly sinuous superhelical structure, clamping around the elongated SCF scaffold protein Cul1. At one end, a Cand1 beta hairpin protrusion partially occupies the adaptor binding site on Cul1, inhibiting its interactions with the Skp1 adaptor and the substrate-recruiting F box protein subunits. At the other end, two Cand1 HEAT repeats pack against a conserved Cul1 surface cleft and bury a Cul1 lysine residue, whose modification by the ubiquitin-like protein, Nedd8, is able to block Cand1-Cul1 association. Together with biochemical evidence, these structural results elucidate the mechanisms by which Cand1 and Nedd8 regulate the assembly-disassembly cycles of SCF and other cullin-dependent E3 complexes.

PubMed: 15537541
DOI: 10.1016/j.cell.2004.10.019

Experimental method

X-RAY DIFFRACTION (3.1 Å)