3R9I

2.6A resolution structure of MinD complexed with MinE (12-31) peptide

3R9I の概要

• エントリーDOI: 10.2210/pdb3r9i/pdb
• 関連するPDBエントリー: 3Q9L 3R9J
• 分子名称: Septum site-determining protein minD, Cell division topological specificity factor, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: atpase, bacterial cell division inhibitor, mine, cell cycle, hydrolase-cell cycle complex, hydrolase/cell cycle
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein: P0AEZ3
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 125254.67

構造登録者

Lovell, S.,Battaile, K.P.,Park, K.-T.,Wu, W.,Holyoak, T.,Lutkenhaus, J. (登録日: 2011-03-25, 公開日: 2011-08-17, 最終更新日: 2023-09-13)

主引用文献

Park, K.T.,Wu, W.,Battaile, K.P.,Lovell, S.,Holyoak, T.,Lutkenhaus, J.
The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.
Cell(Cambridge,Mass.), 146:396-407, 2011

PubMed Abstract: In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear because the MinD-binding regions of MinE are sequestered within a six-stranded β sheet and masked by N-terminal helices. minE mutations that restore interaction between some MinD and MinE mutants were isolated. These mutations alter the MinE structure leading to release of the MinD-binding regions and the N-terminal helices that bind the membrane. Crystallization of MinD-MinE complexes revealed a four-stranded β sheet MinE dimer with the released β strands (MinD-binding regions) converted to α helices bound to MinD dimers. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface.

PubMed: 21816275
DOI: 10.1016/j.cell.2011.06.042

実験手法

X-RAY DIFFRACTION (2.6 Å)