2MC3

NMR solution structure of the winged-helix domain from MUS81 structure-specific endonuclease

2MC3 の概要

• エントリーDOI: 10.2210/pdb2mc3/pdb
• NMR情報: BMRB: 17324
• 分子名称: MUS81 endonuclease homolog (Yeast), isoform CRA_b (1 entity in total)
• 機能のキーワード: alpha beta, winged-helix, dna binding, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12006.80

構造登録者

Harris, R.,Fadden, A.,Mcdonald, N.Q. (登録日: 2013-08-14, 公開日: 2013-09-18, 最終更新日: 2024-05-15)

主引用文献

Fadden, A.J.,Schalbetter, S.,Bowles, M.,Harris, R.,Lally, J.,Carr, A.M.,McDonald, N.Q.
A winged helix domain in human MUS81 binds DNA and modulates the endonuclease activity of MUS81 complexes.
Nucleic Acids Res., 41:9741-9752, 2013

PubMed Abstract: The MUS81-EME1 endonuclease maintains metazoan genomic integrity by cleaving branched DNA structures that arise during the resolution of recombination intermediates. In humans, MUS81 also forms a poorly characterized complex with EME2. Here, we identify and determine the structure of a winged helix (WH) domain from human MUS81, which binds DNA. WH domain mutations greatly reduce binding of the isolated domain to DNA and impact on incision activity of MUS81-EME1/EME2 complexes. Deletion of the WH domain reduces the endonuclease activity of both MUS81-EME1 and MUS81-EME2 complexes, and incisions made by MUS81-EME2 are made closer to the junction on substrates containing a downstream duplex, such as fork structures and nicked Holliday junctions. WH domain mutation or deletion in Schizosaccharomyces pombe phenocopies the DNA-damage sensitivity of strains deleted for mus81. Our results indicate an important role for the WH domain in both yeast and human MUS81 complexes.

PubMed: 23982516
DOI: 10.1093/nar/gkt760

実験手法

SOLUTION NMR