| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2036325 | Cell | 2011 | 12 Pages |
SummaryIn 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.PaperFlick To view the video inline, enable JavaScript on your browser. However, you can download and view the video by clicking on the icon belowHelp with MP4 filesOptionsDownload video (11536 K)
Graphical AbstractFigure optionsDownload full-size imageDownload high-quality image (367 K)Download as PowerPoint slideHighlights► Interaction of MinE with MinD requires dramatic conformational changes in MinE ► Upon sensing MinD, MinE releases a β strand and a membrane-targeting sequence (MTS) ► The β strand forms an α helix bound to MinD and the MTS binds the membrane ► A Tarzan of the jungle model is proposed for MinE transferring between MinDs
