2MC3

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

Summary for 2MC3

• Entry DOI: 10.2210/pdb2mc3/pdb
• NMR Information: BMRB: 17324
• Descriptor: MUS81 endonuclease homolog (Yeast), isoform CRA_b (1 entity in total)
• Functional Keywords: alpha beta, winged-helix, dna binding, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 12006.80

Authors

Harris, R.,Fadden, A.,Mcdonald, N.Q. (deposition date: 2013-08-14, release date: 2013-09-18, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR