4PPE

human RNF4 RING domain

Summary for 4PPE

• Entry DOI: 10.2210/pdb4ppe/pdb
• Descriptor: E3 ubiquitin-protein ligase RNF4, ZINC ION (3 entities in total)
• Functional Keywords: ring domain, ubiquitin ligase, ligase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P78317
• Total number of polymer chains: 2
• Total formula weight: 16794.78

Authors

Perry, J.J.,Arvai, A.S.,Hitomi, C.,Tainer, J.A. (deposition date: 2014-02-26, release date: 2014-03-26, Last modification date: 2024-02-28)

Primary citation

Groocock, L.M.,Nie, M.,Prudden, J.,Moiani, D.,Wang, T.,Cheltsov, A.,Rambo, R.P.,Arvai, A.S.,Hitomi, C.,Tainer, J.A.,Luger, K.,Perry, J.J.,Lazzerini-Denchi, E.,Boddy, M.N.
RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response.
Embo Rep., 15:601-608, 2014

PubMed Abstract: The post-translational modification of DNA repair and checkpoint proteins by ubiquitin and small ubiquitin-like modifier (SUMO) critically orchestrates the DNA damage response (DDR). The ubiquitin ligase RNF4 integrates signaling by SUMO and ubiquitin, through its selective recognition and ubiquitination of SUMO-modified proteins. Here, we define a key new determinant for target discrimination by RNF4, in addition to interaction with SUMO. We identify a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones. Furthermore, RNF4 nucleosome-targeting is crucially required for the repair of TRF2-depleted dysfunctional telomeres by 53BP1-mediated non-homologous end joining.

PubMed: 24714598
DOI: 10.1002/embr.201338369

Experimental method

X-RAY DIFFRACTION (2 Å)