Abstract
Correct positioning of the division septum in Escherichia coli depends on the coordinated action of the MinC, MinD and MinE proteins. Topological specificity is conferred on the MinCD division inhibitor by MinE, which counters MinCD activity only in the vicinity of the preferred midcell division site. Here we report the structure of the homodimeric topological specificity domain of Escherichia coli MinE and show that it forms a novel αβ sandwich. Structure-directed mutagenesis of conserved surface residues has enabled us to identify a spatially restricted site on the surface of the protein that is critical for the topological specificity function of MinE.
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Acknowledgements
This work was supported by an NIH grant to L.I.R. and a grant from the Australian NHMRC to G.F.K. S.L.R. was supported in part by an HFSP Long Term Fellowship. Thanks to S. Robson and M.J. Osborn for help with graphics and for critical proofreading, respectively. Preliminary sequence data was obtained from The Institute for Genomic Research website at http://www.tigr.org.
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King, G., Shih, YL., Maciejewski, M. et al. Structural basis for the topological specificity function of MinE. Nat Struct Mol Biol 7, 1013–1017 (2000). https://doi.org/10.1038/80917
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DOI: https://doi.org/10.1038/80917
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