title: Structure of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ.
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.
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
authors.forename: Christopher H S
authors.initials: CH
authors.lastname: Aylett
authors.forename: Thierry
authors.initials: T
authors.lastname: Izoré
authors.forename: Linda A
authors.initials: LA
authors.lastname: Amos
authors.forename: Jan
authors.initials: J
authors.lastname: Löwe
mesh_terms: D000595:Amino Acid Sequence; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D017105:Pseudomonas Phages / Q000737:chemistry*; D016415:Sequence Alignment; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D014764:Viral Proteins