9BI4

cryo EM structure of dsDNA bound Mre11-Rad50 complex

Summary for 9BI4

• Entry DOI: 10.2210/pdb9bi4/pdb
• EMDB information: 44558
• Descriptor: DNA repair protein RAD50, Double-strand break repair protein MRE11, one strand of dsDNA, ... (7 entities in total)
• Functional Keywords: mrn, mre11, rad50, nbs1, dna binding, dna damage, dna repair, dna binding protein
• Biological source: Saccharomyces cerevisiae (brewer's yeast); More
• Total number of polymer chains: 6
• Total formula weight: 517246.93

Authors

Yu, Y.,Patel, D.J. (deposition date: 2024-04-22, release date: 2025-01-15)

Primary citation

Petrini, J.,Hohl, M.,Yu, Y.,Kuryavyi, V.,Patel, D.
Structure guided functional analysis of the S. cerevisiae Mre11 complex.
Res Sq, 2024

PubMed Abstract: The Mre11 complex comprises Mre11, Rad50 and Nbs1 (Xrs2 in ). The core components, Mre11 and Rad50 are highly conserved, with readily identifiable orthologs in all clades of life, whereas Nbs1/Xrs2 are present only in eukaryotes. In eukaryotes, the complex is integral to the DNA damage response, acting in DNA double strand break (DSB) detection and repair, and the activation of DNA damage signaling. We present here a 3.2 Å cryo-EM structure of the Mre11-Rad50 complex with bound dsDNA. The structure provided a foundation for detailed mutational analyses regarding homo and heterotypic protein interfaces, as well as DNA binding properties of Rad50. We define several conserved residues in Rad50 and Mre11 that are critical to complex assembly as well as for DNA binding. In addition, the data reveal that the Rad50 coiled coil domain influences ATP hydrolysis over long distances.

PubMed: 39711558
DOI: 10.21203/rs.3.rs-5390974/v1

Experimental method

ELECTRON MICROSCOPY (3.2 Å)