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 DOI Help

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

Open Access Open Access

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

Subject Areas: Biology and Bio-materials


Instruments: B21-High Throughput SAXS

Documents:
s41598-019-54999-x.pdf

Discipline Tags:



Technical Tags: