2B5M

Crystal Structure of DDB1

Summary for 2B5M

• Entry DOI: 10.2210/pdb2b5m/pdb
• Related: 2B5L 2B5N
• Descriptor: damage-specific DNA binding protein 1 (1 entity in total)
• Functional Keywords: ddb1, beta-propeller, propeller cluster, dna binding protein-protein binding complex, dna binding protein/protein binding
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 127117.50

Authors

Li, T.,Chen, X.,Garbutt, K.C.,Zhou, P.,Zheng, N. (deposition date: 2005-09-28, release date: 2006-02-28, Last modification date: 2024-11-06)

Primary citation

Li, T.,Chen, X.,Garbutt, K.C.,Zhou, P.,Zheng, N.
Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase.
Cell(Cambridge,Mass.), 124:105-117, 2006

PubMed Abstract: The DDB1-Cul4A ubiquitin ligase complex promotes protein ubiquitination in diverse cellular functions and is reprogrammed by the V proteins of paramyxoviruses to degrade STATs and block interferon signaling. Here we report the crystal structures of DDB1 alone and in complex with the simian virus 5 V protein. The DDB1 structure reveals an intertwined three-propeller cluster, which contains two tightly coupled beta propellers with a large pocket in between and a third beta propeller flexibly attached on the side. The rigid double-propeller fold of DDB1 is targeted by the viral V protein, which inserts an entire helix into the double-propeller pocket, whereas the third propeller domain docks DDB1 to the N terminus of the Cul4A scaffold. Together, these results not only provide structural insights into how the virus hijacks the DDB1-Cul4A ubiquitin ligase but also establish a structural framework for understanding the multiple functions of DDB1 in the uniquely assembled cullin-RING E3 machinery.

PubMed: 16413485
DOI: 10.1016/j.cell.2005.10.033

Experimental method

X-RAY DIFFRACTION (2.92 Å)