4NDY

Human MHF1-MHF2 DNA complex

Summary for 4NDY

• Entry DOI: 10.2210/pdb4ndy/pdb
• Related: 4NE1
• Descriptor: DNA (26-MER), Centromere protein S, Centromere protein X, ... (4 entities in total)
• Functional Keywords: histone fold, dna repair, genome maintenance, centromere construction, fanconi anemia, fancm, nucleus, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q8N2Z9 A8MT69
• Total number of polymer chains: 24
• Total formula weight: 236832.40

Authors

Zhao, Q.,Saro, D.,Sachpatzidis, A.,Sung, P.,Xiong, Y. (deposition date: 2013-10-28, release date: 2014-01-22, Last modification date: 2024-02-28)

Primary citation

Zhao, Q.,Saro, D.,Sachpatzidis, A.,Singh, T.R.,Schlingman, D.,Zheng, X.F.,Mack, A.,Tsai, M.S.,Mochrie, S.,Regan, L.,Meetei, A.R.,Sung, P.,Xiong, Y.
The MHF complex senses branched DNA by binding a pair of crossover DNA duplexes.
Nat Commun, 5:2987-2987, 2014

PubMed Abstract: The conserved MHF1-MHF2 (MHF) complex functions in the activation of the Fanconi anaemia pathway of the DNA damage response, in regulating homologous recombination, and in DNA replication fork maintenance. MHF facilitates the processing of multiple types of branched DNAs by the DNA translocase FANCM. Here we report the crystal structure of a human MHF-DNA complex that reveals the DNA-binding mode of MHF. The structure suggests that MHF prefers branched DNA over double-stranded DNA because it engages two duplex arms. Biochemical analyses verify that MHF preferentially engages DNA forks or various four-way junctions independent of the junction-site structure. Furthermore, genetic experiments provide evidence that the observed DNA-binding interface of MHF is important for cellular resistance to DNA damage. These results offer insights into how the MHF complex recognizes branched DNA and stimulates FANCM activity at such a structure to promote genome maintenance.

PubMed: 24390579
DOI: 10.1038/ncomms3987

Experimental method

X-RAY DIFFRACTION (6.999 Å)