3Q9L

The structure of the dimeric E.coli MinD-ATP complex

3Q9L の概要

• エントリーDOI: 10.2210/pdb3q9l/pdb
• 分子名称: Septum site-determining protein minD, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: atpase, bacterial cell division inhibitor, minc, mine, cell cycle, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein: P0AEZ3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58064.28

構造登録者

Wu, W.,Park, K.-T.,Lutkenhaus, J.,Holyoak, T. (登録日: 2011-01-08, 公開日: 2011-01-26, 最終更新日: 2024-02-21)

主引用文献

Wu, W.,Park, K.T.,Holyoak, T.,Lutkenhaus, J.
Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.
Mol.Microbiol., 79:1515-1528, 2011

PubMed Abstract: The three Min proteins spatially regulate Z ring positioning in Escherichia coli and are dynamically associated with the membrane. MinD binds to vesicles in the presence of ATP and can recruit MinC or MinE. Biochemical and genetic evidence indicate the binding sites for these two proteins on MinD overlap. Here we solved the structure of a hydrolytic-deficient mutant of MinD truncated for the C-terminal amphipathic helix involved in binding to the membrane. The structure solved in the presence of ATP is a dimer and reveals the face of MinD abutting the membrane. Using a combination of random and extensive site-directed mutagenesis additional residues important for MinE and MinC binding were identified. The location of these residues on the MinD structure confirms that the binding sites overlap and reveals that the binding sites are at the dimer interface and exposed to the cytosol. The location of the binding sites at the dimer interface offers a simple explanation for the ATP dependence of MinC and MinE binding to MinD.

PubMed: 21231967
DOI: 10.1111/j.1365-2958.2010.07536.x

実験手法

X-RAY DIFFRACTION (2.343 Å)