Oxford Events, the new replacement for OxTalks, will launch on 16th March. From now until the launch of Oxford Events, new events cannot be published or edited on OxTalks while all existing records are migrated to the new platform. The existing OxTalks site will remain available to view during this period.
From 16th, Oxford Events will launch on a new website: events.ox.ac.uk, and event submissions will resume. You will need a Halo login to submit events. Full details are available on the Staff Gateway.
Tailed bacteriophages (order Caudovirales) are characterised by an icosahedral capsid, which encloses a double-stranded DNA genome. These phages and herpesviruses share a common assembly pathway for prohead formation and genome packaging. In both viruses, DNA incorporation and ejection is mediated by a machinery built by similar components, including the portal protein and a motor protein complex called terminase, which provides the energy for DNA translocation and has nuclease activity. The portal is a large oligomeric ring-shaped protein located at a unique pentameric vertex of the capsid. It acts as an initiator for capsid assembly and it is also a critical part of the DNA packaging and ejection machinery. In phages, the portal is also involved in tail assembly.
Using X-ray crystallography and high-resolution cryo-electron microscopy, we have solved the structure of a bacteriophage portal, in different conformations, and a tail complex. Our findings point to a molecular mechanism for DNA retention and ejection. A herpesvirus terminase subunit and a portal have also been solved and will be compared with their phage equivalent parts.
