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Nano-encapsulated escherichia coli divisome anchor ZipA, and in complex with FtsZ
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Lee, Sarah C., Collins, Richard, Lin, Yu-pin, Jamshad, Mohammed, Broughton, Claire E., Harris, Sarah A., Hanson, Benjamin S, Tognoloni, Cecilia, Parslow, Rosemary A., Terry, Ann E., Rodger, Alison, Smith, Corinne J., Edler, Karen J., Ford, Robert, Roper, David I. and Dafforn, Timothy R. (2019) Nano-encapsulated escherichia coli divisome anchor ZipA, and in complex with FtsZ. Scientific Reports, 9 (1). 18712. doi:10.1038/s41598-019-54999-x ISSN 2045-2322.
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WRAP-nano-encapsulated-divisome-anchor-complex-FtsZ-Roper-2019.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (2551Kb) | Preview |
Official URL: http://dx.doi.org/10.1038/s41598-019-54999-x
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.
Item Type: | Journal Article | ||||||
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Subjects: | Q Science > QH Natural history Q Science > QP Physiology Q Science > QR Microbiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||
Library of Congress Subject Headings (LCSH): | Escherichia coli, Membrane proteins -- Research, Cell division -- Research, Lipids -- Research | ||||||
Journal or Publication Title: | Scientific Reports | ||||||
Publisher: | Nature Publishing Group | ||||||
ISSN: | 2045-2322 | ||||||
Official Date: | 10 December 2019 | ||||||
Dates: |
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Volume: | 9 | ||||||
Number: | 1 | ||||||
Article Number: | 18712 | ||||||
DOI: | 10.1038/s41598-019-54999-x | ||||||
Status: | Peer Reviewed | ||||||
Publication Status: | Published | ||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||
Date of first compliant deposit: | 16 December 2019 | ||||||
Date of first compliant Open Access: | 16 December 2019 | ||||||
RIOXX Funder/Project Grant: |
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