8h1p
From Proteopedia
Cryo-EM structure of the human RAD52 protein
Structural highlights
FunctionRAD52_HUMAN Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.[1] Publication Abstract from PubMedThe 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-oligomerization 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-oligomerization has remained elusive. In the present study, we determined the solution structure of the human RAD52 protein by cryo-electron microscopy (cryo-EM), at an average resolution of 3.5 A. 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. The cryo-EM structure of full-length RAD52 protein contains an undecameric ring.,Kinoshita C, Takizawa Y, Saotome M, Ogino S, Kurumizaka H, Kagawa W FEBS Open Bio. 2023 Jan 27. doi: 10.1002/2211-5463.13565. PMID:36707939[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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