3V9R

Crystal structure of Saccharomyces cerevisiae MHF complex

3V9R の概要

• エントリーDOI: 10.2210/pdb3v9r/pdb
• 分子名称: Uncharacterized protein YOL086W-A, Uncharacterized protein YDL160C-A, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: mhf1, mhf2, histone fold, fanconi anemia, dna repair, dna binding protein
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 42237.64

構造登録者

Yang, H.,Zhang, T.,Zhong, C.,Li, H.,Zhou, J.,Ding, J. (登録日: 2011-12-28, 公開日: 2012-02-29, 最終更新日: 2024-10-30)

主引用文献

Yang, H.,Zhang, T.,Tao, Y.,Wu, L.,Li, H.T.,Zhou, J.Q.,Zhong, C.,Ding, J.
Saccharomyces Cerevisiae MHF Complex Structurally Resembles the Histones (H3-H4)(2) Heterotetramer and Functions as a Heterotetramer
Structure, 20:364-370, 2012

PubMed Abstract: Fanconi anemia (FA) is a chromosomal instability disorder associated with deficiencies in the Fanconi anemia complementation group (FANC) network. A complex consisting of FANCM-associated histone-fold proteins 1 and 2 (MHF1 and MHF2) has been shown to act cooperatively with FANCM in DNA damage repair in the FA pathway. Here we report the structure of Saccharomyces cerevisiae MHF complex in which MHF1 and MHF2 assume a typical histone fold, and the complex has a heterotetrameric architecture similar to that of the histones (H3-H4)₂ heterotetramer. Loop L2 of MHF1 is probably involved in DNA binding, and loop L3 and helices α2 and α3 of one MHF1 subunit interact with those of the other to form two heterotetramer interfaces. Further genetic data demonstrate that the heterotetramer assembly is essential for the function of the complex in DNA repair. These results provide, to the best of our knowledge, new mechanistic insights into the function of the MHF complex.

PubMed: 22325783
DOI: 10.1016/j.str.2011.12.012

実験手法

X-RAY DIFFRACTION (2.4 Å)