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Structure and function of a spectrin-like regulator of bacterial cytokinesis

DOI: 10.1038/ncomms6421 DOI Help
PMID: 25403286 PMID Help

Authors: Robert Cleverley (Newcastle University) , Jeffrey R. Barrett (University of Wollongong) , Arnaud Basle (University of Newcastle Upon Tyne) , Nhat Khai Bui (Newcastle University) , Lorraine Hewitt (University of Newcastle) , Alexandra Solovyova (Newcastle University) , Zhi-qiang Xu (University of Wollongong) , Richard A. Daniel (Newcastle University) , Nicholas E. Dixon (University of Wollongong) , Elizabeth J. Harry (The ithree Institute, University of Technology, Sydney, New South Wales) , Aaron J. Oakley (University of Wollongong) , Waldemar Vollmer (Newcastle University) , Rick Lewis (Newcastle University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 5

State: Published (Approved)
Published: November 2014
Diamond Proposal Number(s): 9948

Open Access Open Access

Abstract: Bacterial cell division is facilitated by a molecular machineĀ—the divisomeĀ—that assembles at mid-cell in dividing cells. The formation of the cytokinetic Z-ring by the tubulin homologue FtsZ is regulated by several factors, including the divisome component EzrA. Here we describe the structure of the 60-kDa cytoplasmic domain of EzrA, which comprises five linear repeats of an unusual triple helical bundle. The EzrA structure is bent into a semicircle, providing the protein with the potential to interact at both N- and C-termini with adjacent membrane-bound divisome components. We also identify at least two binding sites for FtsZ on EzrA and map regions of EzrA that are responsible for regulating FtsZ assembly. The individual repeats, and their linear organization, are homologous to the spectrin proteins that connect actin filaments to the membrane in eukaryotes, and we thus propose that EzrA is the founding member of the bacterial spectrin family.

Subject Areas: Biology and Bio-materials

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Other Facilities: Australian Synchrotron

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