3NG2

Crystal structure of the RNF4 ring domain dimer

Summary for 3NG2

• Entry DOI: 10.2210/pdb3ng2/pdb
• Descriptor: RING finger protein 4, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ring domain, e3 ligase, ubiquitylation, sumoylation, zinc-finger, metal binding protein
• Biological source: Rattus norvegicus (rat)
• Cellular location: Cytoplasm: O88846
• Total number of polymer chains: 2
• Total formula weight: 16127.99

Authors

Liew, C.W.,Day, C.L. (deposition date: 2010-06-10, release date: 2010-10-06, Last modification date: 2024-03-20)

Primary citation

Liew, C.W.,Sun, H.,Hunter, T.,Day, C.L.
RING domain dimerization is essential for RNF4 function
Biochem.J., 431:23-29, 2010

PubMed Abstract: RNF4 [RING (really interesting new gene) finger protein 4] family ubiquitin ligases are RING E3 ligases that regulate the homoeostasis of SUMOylated proteins by promoting their ubiquitylation. In the present paper we report that the RING domain of RNF4 forms a stable dimer, and that dimerization is required for ubiquitin transfer. Our results suggest that the stability of the E2~ubiquitin thioester bond is regulated by RING domain dimerization.

PubMed: 20681948
DOI: 10.1042/BJ20100957

Experimental method

X-RAY DIFFRACTION (1.8 Å)