Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ
(2019) In Scientific Reports 9(1).- 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... (More) - 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/46c71106-af82-422b-bf36-24577544fe93
- author
- organization
- publishing date
- 2019-12-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Scientific Reports
- volume
- 9
- issue
- 1
- article number
- 18712
- pages
- 16 pages
- publisher
- Nature Publishing Group
- external identifiers
-
- scopus:85076378530
- pmid:31822696
- ISSN
- 2045-2322
- DOI
- 10.1038/s41598-019-54999-x
- language
- English
- LU publication?
- yes
- additional info
- Publisher Copyright: © 2019, The Author(s).
- id
- 46c71106-af82-422b-bf36-24577544fe93
- date added to LUP
- 2023-01-18 09:04:57
- date last changed
- 2024-04-04 07:54:59
@article{46c71106-af82-422b-bf36-24577544fe93, abstract = {{The <i>E</i>. <i>coli</i> membrane protein ZipA, binds to the tubulin <br> homologue FtsZ, in the early stage of cell division. We isolated ZipA in<br> a Styrene Maleic Acid lipid particle (SMALP) preserving its position <br> and integrity with native <i>E</i>. <i>coli</i> membrane lipids. Direct <br> binding of ZipA to FtsZ is demonstrated, including FtsZ fibre bundles <br> decorated with ZipA. Using Cryo-Electron Microscopy, small-angle X-ray <br> and neutron scattering, we determine the encapsulated-ZipA structure in <br> isolation, and in complex with FtsZ to a resolution of 1.6 nm. Three <br> regions can be identified from the structure which correspond to, SMALP <br> encapsulated membrane and ZipA transmembrane helix, a separate short <br> compact tether, and ZipA globular head which binds FtsZ. The complex <br> extends 12 nm from the membrane in a compact structure, supported by <br> mesoscale modelling techniques, measuring the movement and stiffness of <br> the regions within ZipA provides molecular scale analysis and <br> visualisation of the early divisome.}}, author = {{Lee, Sarah C. and Collins, Richard and Lin, Yu-pin and Jamshad, Mohammed and Broughton, Claire and Harris, Sarah A. and Hanson, Benjamin S. and Tognoloni, Cecilia and Parslow, Rosemary A. and Terry, Ann E. and Rodger, Alison and Smith, Corinne J. and Edler, Karen J. and Ford, Robert and Roper, David I. and Dafforn, Timothy R.}}, issn = {{2045-2322}}, language = {{eng}}, month = {{12}}, number = {{1}}, publisher = {{Nature Publishing Group}}, series = {{Scientific Reports}}, title = {{Nano-encapsulated <i>Escherichia coli</i> Divisome Anchor ZipA, and in Complex with FtsZ}}, url = {{http://dx.doi.org/10.1038/s41598-019-54999-x}}, doi = {{10.1038/s41598-019-54999-x}}, volume = {{9}}, year = {{2019}}, }