Publication
Article Metrics
Citations
Online attention
Nano-encapsulated Escherichia coli divisome anchor ZipA, and in complex with FtsZ
DOI:
10.1038/s41598-019-54999-x
Authors:
Sarah C.
Lee
(University of Birmingham)
,
Richard
Collins
(The University of Manchester)
,
Yu-Pin
Lin
(University of Birmingham)
,
Mohammed
Jamshad
(University of Birmingham)
,
Claire
Broughton
(University of Warwick)
,
Sarah A.
Harris
(University of Leeds)
,
Benjamin S.
Hanson
(University of Leeds)
,
Cecilia
Tognoloni
(University of Bath)
,
Rosemary A.
Parslow
(University of Birmingham)
,
Ann E.
Terry
(MAX IV Laboratory Lund University)
,
Alison
Rodger
(Macquarie University)
,
Corinne J.
Smith
(University of Warwick)
,
Karen J.
Edler
(University of Bath)
,
Robert
Ford
(University of Manchester)
,
David I.
Roper
(University of Warwick)
,
Timothy R.
Dafforn
(University of Birmingham)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Scientific Reports
, VOL 9
State:
Published (Approved)
Published:
December 2019
Diamond Proposal Number(s):
9727

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.
Journal Keywords: Cellular microbiology; Cryoelectron microscopy; Membrane structure and assembly
Diamond Keywords: Bacteria
Subject Areas:
Biology and Bio-materials,
Chemistry
Instruments:
B21-High Throughput SAXS
Added On:
16/12/2019 12:09
Documents:
s41598-019-54999-x.pdf
Discipline Tags:
Biochemistry
Chemistry
Structural biology
Life Sciences & Biotech
Technical Tags:
Scattering
Small Angle X-ray Scattering (SAXS)