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Folded domains of Xrs2 from S.cerevisiae
Structural highlights
FunctionXRS2_YEAST Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:14522986, PubMed:1468624, PubMed:35501303). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:35501303). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the MRN complex, XRS2 acts as a protein-protein adapter (PubMed:14522986). Specifically recognizes and binds phosphorylated proteins, promoting their recruitment to DNA damage sites (By similarity). Recruits MRE11 and RAD50 components of the MRN complex to DNA damage sites in response to DNA damage (PubMed:14522986). The MRN complex is also required for the processing of R-loops (PubMed:31537797).[UniProtKB:O60934][1] [2] [3] [4] Publication Abstract from PubMedThe 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 A 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. Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae.,Vigneswaran A, Shi K, Aihara H, Evans RL 3rd, Latham MP Acta Crystallogr F Struct Biol Commun. 2025 Sep 1;81(Pt 9):365-373. doi: , 10.1107/S2053230X25006867. Epub 2025 Aug 6. PMID:40767353[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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