3R9I
2.6A resolution structure of MinD complexed with MinE (12-31) peptide
Summary for 3R9I
| Entry DOI | 10.2210/pdb3r9i/pdb |
| Related | 3Q9L 3R9J |
| Descriptor | Septum site-determining protein minD, Cell division topological specificity factor, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | atpase, bacterial cell division inhibitor, mine, cell cycle, hydrolase-cell cycle complex, hydrolase/cell cycle |
| Biological source | Escherichia coli More |
| Cellular location | Cell inner membrane; Peripheral membrane protein: P0AEZ3 |
| Total number of polymer chains | 8 |
| Total formula weight | 125254.67 |
| Authors | Lovell, S.,Battaile, K.P.,Park, K.-T.,Wu, W.,Holyoak, T.,Lutkenhaus, J. (deposition date: 2011-03-25, release date: 2011-08-17, Last modification date: 2023-09-13) |
| Primary citation | 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 Cited by 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: 21816275DOI: 10.1016/j.cell.2011.06.042 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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