Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae

2025/08/05 by Ajeak Vigneswaran, Ke Shi, Hideki Aihara +2 · 1 voice
Biochemistry, Genetics and Molecular Biology · Materials Science · #DNA Repair Mechanisms #Enzyme Structure and Function #Photosynthetic Processes and Mechanisms

paper · pdf · doi:10.1107/s2053230x25006867

openalex publication_date 2025/08/05 · openalex created_date 2025/08/06 · openalex updated_date 2026/06/26

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.

Citations

• The MRN complex in double‐strand break repair and telomere maintenance
• Highly accurate protein structure prediction with AlphaFold
• Highly accurate protein structure prediction for the human proteome
• The CCP 4 suite: integrative software for macromolecular crystallography

Discussions

• The first high-resolution structure of the folded domains of Xrs2 from S. cerevisiae will advance understanding of its functions in the DNA damage response and telomere-length maintenance @UMNews #Nbs [bsky, 2 points, 0 comments]

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