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Structure of the Tubulin/FtsZ-Like Protein TubZ from Pseudomonas Bacteriophage ΦKZ

DOI: 10.1016/j.jmb.2013.03.019 DOI Help
PMID: 23528827 PMID Help

Authors: Christopher Aylett (MRC Laboratory of Molecular Biology) , Thierry Izore (MRC Laboratory of Molecular Biology) , Linda Amos (MRC Laboratory of Molecular Biology) , Jan Lowe (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Molecular Biology , VOL 425 (12) , PAGES 2164 - 2173

State: Published (Approved)
Published: March 2013
Diamond Proposal Number(s): 8547

Open Access Open Access

Abstract: Pseudomonas ΦKZ-like bacteriophages encode a group of related tubulin/FtsZ-like proteins believed to be essential for the correct centring of replicated bacteriophage virions within the bacterial host. In this study, we present crystal structures of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ in both the monomeric and protofilament states, revealing that ΦKZ TubZ undergoes structural changes required to polymerise, forming a canonical tubulin/FtsZ-like protofilament. Combining our structures with previous work, we propose a polymerisation–depolymerisation cycle for the Pseudomonas bacteriophage subgroup of tubulin/FtsZ-like proteins. Electron cryo-microscopy of ΦKZ TubZ filaments polymerised in vitro implies a long-pitch helical arrangement for the constituent protofilaments. Intriguingly, this feature is shared by the other known subgroup of bacteriophage tubulin/FtsZ-like proteins from Clostridium species, which are thought to be involved in partitioning the genomes of bacteriophages adopting a pseudo-lysogenic life cycle.

Journal Keywords: Cryoelectron; Crystallography; X-Ray; Models; Molecular; Protein; Pseudomonas; Sequence; Viral Proteins

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Other Facilities: Yes, ESRF

Added On: 23/09/2013 14:08

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