9EE7
Folded domains of Xrs2 from S.cerevisiae
Summary for 9EE7
| Entry DOI | 10.2210/pdb9ee7/pdb |
| Descriptor | DNA repair protein XRS2 (2 entities in total) |
| Functional Keywords | dna repair, protein binding |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 37172.78 |
| Authors | Vigneswaran, A.,Shi, K.,Evans, R.,Aihara, H.,Latham, M.P. (deposition date: 2024-11-18, release date: 2025-09-10) |
| Primary citation | Vigneswaran, A.,Shi, K.,Aihara, H.,Evans 3rd, R.L.,Latham, M.P. Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae. Acta Crystallogr.,Sect.F, 81:365-373, 2025 Cited by PubMed 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. PubMed: 40767353DOI: 10.1107/S2053230X25006867 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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