4EOZ

Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain

Summary for 4EOZ

• Entry DOI: 10.2210/pdb4eoz/pdb
• Descriptor: Speckle-type POZ protein, Cullin-3 (3 entities in total)
• Functional Keywords: e3 ubiquitin ligase, nucleus, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: O43791 Q13618
• Total number of polymer chains: 4
• Total formula weight: 119258.49

Authors

Prive, G.G.,Errington, W.J. (deposition date: 2012-04-16, release date: 2012-05-30, Last modification date: 2013-01-09)

Primary citation

Errington, W.J.,Khan, M.Q.,Bueler, S.A.,Rubinstein, J.L.,Chakrabartty, A.,Prive, G.G.
Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase.
Structure, 20:1141-1153, 2012

PubMed Abstract: The E3 ligases recruit substrate proteins for targeted ubiquitylation. Recent insights into the mechanisms of ubiquitylation demonstrate that E3 ligases can possess active regulatory properties beyond those of a simple assembly scaffold. Here, we describe the dimeric structure of the E3 ligase adaptor protein SPOP (speckle-type POZ protein) in complex with the N-terminal domain of Cul3 at 2.4 Å resolution. We find that SPOP forms large oligomers that can form heteromeric species with the closely related paralog SPOPL. In combination, SPOP and SPOPL (SPOP-like) form a molecular rheostat that can fine-tune E3 ubiquitin ligase activity by affecting the oligomeric state of the E3 complex. We propose that adaptor protein self-assembly provides a graded level of regulation of the SPOP/Cul3 E3 ligase toward its multiple protein substrates.

PubMed: 22632832
DOI: 10.1016/j.str.2012.04.009

Experimental method

X-RAY DIFFRACTION (2.4 Å)