3MVB

Crystal structure of a triple RFY mutant of human MTERF1 bound to the termination sequence

3MVB の概要

• エントリーDOI: 10.2210/pdb3mvb/pdb
• 関連するPDBエントリー: 3MVA
• 分子名称: Transcription termination factor, mitochondrial, 5'-D(*AP*TP*TP*AP*CP*CP*GP*GP*GP*CP*TP*CP*TP*GP*CP*CP*AP*TP*CP*TP*TP*A)-3', 5'-D(*TP*AP*AP*GP*AP*TP*GP*GP*CP*AP*GP*AP*GP*CP*CP*CP*GP*GP*TP*AP*AP*T)-3', ... (4 entities in total)
• 機能のキーワード: all alpha-helix, protein-dna, transcription factor, termination, mitochondria, transcription-dna complex, transcription/dna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion: Q99551
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 52574.02

構造登録者

Yakubovskaya, E.,Mejia, E.,Byrnes, J.,Hambardjieva, E.,Garcia-Diaz, M. (登録日: 2010-05-03, 公開日: 2010-06-30, 最終更新日: 2024-02-21)

主引用文献

Yakubovskaya, E.,Mejia, E.,Byrnes, J.,Hambardjieva, E.,Garcia-Diaz, M.
Helix unwinding and base flipping enable human MTERF1 to terminate mitochondrial transcription.
Cell(Cambridge,Mass.), 141:982-993, 2010

PubMed Abstract: Defects in mitochondrial gene expression are associated with aging and disease. Mterf proteins have been implicated in modulating transcription, replication and protein synthesis. We have solved the structure of a member of this family, the human mitochondrial transcriptional terminator MTERF1, bound to dsDNA containing the termination sequence. The structure indicates that upon sequence recognition MTERF1 unwinds the DNA molecule, promoting eversion of three nucleotides. Base flipping is critical for stable binding and transcriptional termination. Additional structural and biochemical results provide insight into the DNA binding mechanism and explain how MTERF1 recognizes its target sequence. Finally, we have demonstrated that the mitochondrial pathogenic G3249A and G3244A mutations interfere with key interactions for sequence recognition, eliminating termination. Our results provide insight into the role of mterf proteins and suggest a link between mitochondrial disease and the regulation of mitochondrial transcription.

PubMed: 20550934
DOI: 10.1016/j.cell.2010.05.018

実験手法

X-RAY DIFFRACTION (2.786 Å)