3Q9L
The structure of the dimeric E.coli MinD-ATP complex
Summary for 3Q9L
| Entry DOI | 10.2210/pdb3q9l/pdb |
| Descriptor | Septum site-determining protein minD, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | atpase, bacterial cell division inhibitor, minc, mine, cell cycle, hydrolase |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Peripheral membrane protein: P0AEZ3 |
| Total number of polymer chains | 2 |
| Total formula weight | 58064.28 |
| Authors | Wu, W.,Park, K.-T.,Lutkenhaus, J.,Holyoak, T. (deposition date: 2011-01-08, release date: 2011-01-26, Last modification date: 2024-02-21) |
| Primary citation | 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 Cited by 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: 21231967DOI: 10.1111/j.1365-2958.2010.07536.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.343 Å) |
Structure validation
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