Publication Abstract from PubMed
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 beta 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 beta sheet MinE dimer with the released beta strands (MinD-binding regions) converted to alpha 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:
The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.,Park KT, Wu W, Battaile KP, Lovell S, Holyoak T, Lutkenhaus J Cell. 2011 Aug 5;146(3):396-407. PMID:21816275[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
