9EE7

Folded domains of Xrs2 from S.cerevisiae

9EE7 の概要

• エントリーDOI: 10.2210/pdb9ee7/pdb
• 分子名称: DNA repair protein XRS2 (2 entities in total)
• 機能のキーワード: dna repair, protein binding
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37172.78

構造登録者

Vigneswaran, A.,Shi, K.,Evans, R.,Aihara, H.,Latham, M.P. (登録日: 2024-11-18, 公開日: 2025-09-10)

主引用文献

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

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: 40767353
DOI: 10.1107/S2053230X25006867

実験手法

X-RAY DIFFRACTION (2.38 Å)