| Literature DB >> 21816275 |
Kyung-Tae Park1, Wei Wu, Kevin P Battaile, Scott Lovell, Todd Holyoak, Joe Lutkenhaus.
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.Entities:
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Year: 2011 PMID： 21816275 PMCID： PMC3155264 DOI： 10.1016/j.cell.2011.06.042
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582