4DRA

Crystal structure of MHF complex

4DRA の概要

• エントリーDOI: 10.2210/pdb4dra/pdb
• 関連するPDBエントリー: 4DRB
• 分子名称: Centromere protein S, Centromere protein X (3 entities in total)
• 機能のキーワード: dna binding complex, dna damage repair, histone-fold, dna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q8N2Z9 A8MT69
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 90330.70

構造登録者

Tao, Y.,Niu, L.,Teng, M. (登録日: 2012-02-17, 公開日: 2012-05-16, 最終更新日: 2024-03-20)

主引用文献

Tao, Y.,Jin, C.,Li, X.,Qi, S.,Chu, L.,Niu, L.,Yao, X.,Teng, M.
The structure of the FANCM-MHF complex reveals physical features for functional assembly
Nat Commun, 3:782-782, 2012

PubMed Abstract: Fanconi anaemia is a rare genetic disease characterized by chromosomal instability and cancer susceptibility. The Fanconi anaemia complementation group protein M (FANCM) forms an evolutionarily conserved DNA-processing complex with MHF1/MHF2 (histone-fold-containing proteins), which is essential for DNA repair in response to genotoxic stress. Here we present the crystal structures of the MHF1-MHF2 complex alone and bound to a fragment of FANCM (FANCM(661-800), designated FANCM-F). The structures show that MHF1 and MHF2 form a compact tetramer to which FANCM-F binds through a 'dual-V' shaped structure. FANCM-F and (MHF1-MHF2)(2) cooperate to constitute a new DNA-binding site that is coupled to the canonical L1L2 region. Perturbation of the MHF-FANCM-F structural plasticity changes the localization of FANCM in vivo. The MHF-FANCM interaction and its subcellular localization are altered by a disease-associated mutant of FANCM. These findings reveal the molecular basis of MHF-FANCM recognition and provide mechanistic insights into the pathway leading to Fanconi anaemia.

PubMed: 22510687
DOI: 10.1038/ncomms1779

実験手法

X-RAY DIFFRACTION (2.414 Å)