4M6W

Crystal structure of the C-terminal segment of FANCM in complex with FAAP24

Summary for 4M6W

• Entry DOI: 10.2210/pdb4m6w/pdb
• Descriptor: Fanconi anemia group M protein, Fanconi anemia-associated protein of 24 kDa, SULFATE ION, ... (4 entities in total)
• Functional Keywords: fancm, faap24, xpf/mus81, fanconi anemia, dna repair, dna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus {ECO:0000269|PubMed:16116422, ECO:0000269|Ref: Q8IYD8; Nucleus : Q9BTP7
• Total number of polymer chains: 2
• Total formula weight: 48818.33

Authors

Yang, H.,Zhang, T.,Tong, L.,Ding, J. (deposition date: 2013-08-11, release date: 2013-10-02, Last modification date: 2024-03-20)

Primary citation

Yang, H.,Zhang, T.,Tao, Y.,Wang, F.,Tong, L.,Ding, J.
Structural insights into the functions of the FANCM-FAAP24 complex in DNA repair.
Nucleic Acids Res., 41:10573-10583, 2013

PubMed Abstract: Fanconi anemia (FA) is a genetically heterogeneous disorder associated with deficiencies in the FA complementation group network. FA complementation group M (FANCM) and FA-associated protein 24 kDa (FAAP24) form a stable complex to anchor the FA core complex to chromatin in repairing DNA interstrand crosslinks. Here, we report the first crystal structure of the C-terminal segment of FANCM in complex with FAAP24. The C-terminal segment of FANCM and FAAP24 both consist of a nuclease domain at the N-terminus and a tandem helix-hairpin-helix (HhH)2 domain at the C-terminus. The FANCM-FAAP24 complex exhibits a similar architecture as that of ApXPF. However, the variations of several key residues and the electrostatic property at the active-site region render a catalytically inactive nuclease domain of FANCM, accounting for the lack of nuclease activity. We also show that the first HhH motif of FAAP24 is a potential binding site for DNA, which plays a critical role in targeting FANCM-FAAP24 to chromatin. These results reveal the mechanistic insights into the functions of FANCM-FAAP24 in DNA repair.

PubMed: 24003026
DOI: 10.1093/nar/gkt788

Experimental method

X-RAY DIFFRACTION (2.9 Å)