8H1P

Cryo-EM structure of the human RAD52 protein

Summary for 8H1P

• Entry DOI: 10.2210/pdb8h1p/pdb
• EMDB information: 34430
• Descriptor: DNA repair protein RAD52 homolog (1 entity in total)
• Functional Keywords: double-strand break repair, single strand annealing protein, dna binding protein, self-oligomerization, recombination
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 11
• Total formula weight: 511664.27

Authors

Kinoshita, C.,Takizawa, Y.,Saotome, M.,Ogino, S.,Kurumizaka, H.,Kagawa, W. (deposition date: 2022-10-03, release date: 2023-02-08, Last modification date: 2024-07-03)

Primary citation

Kinoshita, C.,Takizawa, Y.,Saotome, M.,Ogino, S.,Kurumizaka, H.,Kagawa, W.
The cryo-EM structure of full-length RAD52 protein contains an undecameric ring.
Febs Open Bio, 13:408-418, 2023

PubMed Abstract: The human RAD52 protein, which forms an oligomeric ring structure, is involved in DNA double-strand break repair. The N-terminal half of RAD52 is primarily responsible for self-oligomerisation and DNA binding. Crystallographic studies have revealed the detailed structure of the N-terminal half. However, only low-resolution structures have been reported for the full-length protein, and thus the structural role of the C-terminal half in self-oligomerisation has remained elusive. In this study, we determined the solution structure of the human RAD52 protein by cryo-electron microscopy (cryo-EM), at an average resolution of 3.5 Å. The structure revealed an undecameric ring that is nearly identical to the crystal structures of the N-terminal half. The cryo-EM map for the C-terminal half was poorly defined, indicating that the region is intrinsically disordered. The present cryo-EM structure provides important insights into the mechanistic roles played by the N-terminal and C-terminal halves of RAD52 during DNA double-strand break repair.

PubMed: 36707939
DOI: 10.1002/2211-5463.13565

Experimental method

ELECTRON MICROSCOPY (3.48 Å)