5ZB2

Crystal structure of Rad7 and Elc1 complex in yeast

Summary for 5ZB2

• Entry DOI: 10.2210/pdb5zb2/pdb
• Descriptor: DNA repair protein RAD7, Elongin-C, GLYCEROL, ... (9 entities in total)
• Functional Keywords: lrr, ubiquitin ligase, complex, ligase, dna binding protein-ligase complex, dna binding protein/ligase
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 59272.46

Authors

Jiang, T.,Liu, L.,Huo, Y. (deposition date: 2018-02-09, release date: 2019-02-27, Last modification date: 2024-03-27)

Primary citation

Liu, L.,Huo, Y.,Li, J.,Jiang, T.
Crystal structure of the yeast Rad7-Elc1 complex and assembly of the Rad7-Rad16-Elc1-Cul3 complex.
DNA Repair (Amst.), 77:1-9, 2019

PubMed Abstract: Nucleotide excision repair (NER) is a versatile system that deals with various bulky and helix-distorting DNA lesions caused by UV and environmental mutagens. Based on how lesion recognition occurs, NER has been separated into global genome repair (GGR) and transcription-coupled repair (TCR). The yeast Rad7-Rad16 complex is indispensable for the GGR sub-pathway. Rad7-Rad16 binds to UV-damaged DNA in a synergistic fashion with Rad4, the main lesion recognizer, to achieve efficient recognition of lesions. In addition, Rad7-Rad16 associates with Elc1 and Cul3 to form an EloC-Cul-SOCS-box (ECS)-type E3 ubiquitin ligase complex that ubiquitinates Rad4 in response to UV radiation. However, the structure and architecture of the Rad7-Rad16-Elc1-Cul3 complex remain unsolved. Here, we determined the structure of the Rad7-Elc1 complex and revealed key interaction regions responsible for the formation of the Rad7-Rad16-Elc1-Cul3 complex. These results provide new insights into the assembly of the Rad7-Rad16-Elc1-Cul3 complex and structural framework for further studies.

PubMed: 30840920
DOI: 10.1016/j.dnarep.2019.02.012

Experimental method

X-RAY DIFFRACTION (2.30000538295 Å)