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Article Abstract
The MRE11-RAD50-NBS1/Xrs2 (MRN/X) protein complex acts as a first responder in DNA double-strand break repair and telomere-length maintenance, yet the structural architecture of the yeast ortholog Xrs2 has remained unresolved. In this study, we present the first structure of the folded N-terminal region of Xrs2 from Saccharomyces cerevisiae, resolved at 2.38 Å using X-ray crystallography. Like the previously determined crystal structures of Schizosaccharomyces pombe Nbs1, the folded structure of S. cerevisiae Xrs2 adopts an extended three-domain organization at its N-terminus. Electrostatic analysis reveals two distinct charged patches: a positively charged patch on the FHA domain and a negatively charged patch in the cleft between the FHA and BRCT1 domains. This charge segregation is likely to play a role in mediating interactions with various ligands.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC12400192 | PMC |
| http://dx.doi.org/10.1107/S2053230X25006867 | DOI Listing |
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