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Sci Rep. 2019 Dec 10;9(1):18712. doi: 10.1038/s41598-019-54999-x.

Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ.

Author information

1
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. S.lee.5@bham.ac.uk.
2
Faculty of Life Sciences, A4032 Michael Smith Building, Oxford Road, Manchester, M13 9PT, UK.
3
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
4
School of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.
5
School of Physics and Astronomy and Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, UK.
6
Department of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.
7
MAX IV Laboratory Lund University, P.O. Box 118, SE-221 00, Lund, Sweden.
8
Department of Molecular Sciences, Macquarie University, Macquarie, NSW, 2109, Australia.
9
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. T.R.Dafforn@bham.ac.uk.

Abstract

The E. coli membrane protein ZipA, binds to the tubulin homologue FtsZ, in the early stage of cell division. We isolated ZipA in a Styrene Maleic Acid lipid particle (SMALP) preserving its position and integrity with native E. coli membrane lipids. Direct binding of ZipA to FtsZ is demonstrated, including FtsZ fibre bundles decorated with ZipA. Using Cryo-Electron Microscopy, small-angle X-ray and neutron scattering, we determine the encapsulated-ZipA structure in isolation, and in complex with FtsZ to a resolution of 1.6 nm. Three regions can be identified from the structure which correspond to, SMALP encapsulated membrane and ZipA transmembrane helix, a separate short compact tether, and ZipA globular head which binds FtsZ. The complex extends 12 nm from the membrane in a compact structure, supported by mesoscale modelling techniques, measuring the movement and stiffness of the regions within ZipA provides molecular scale analysis and visualisation of the early divisome.

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