The Department of Biochemistry at the University of Oxford is a centre for world class research and teaching of all aspects of Biochemistry by staff from many different backgrounds and nationalities. Our research addresses a wide range of questions relating to the fundamental basis of all cellular life from man to microbes. This work explains the structures and functions of proteins and nucleic acids, and in doing so addresses the mechanisms of many human diseases. Using this knowledge, other researchers aim to create new vaccines, antiviral and antibacterial therapies to protect and treat humans across the world.
You can read more about the details of our current work and other aspects of the department, including undergraduate teaching and public outreach activities, on these web pages.
Professor Francis Barr, Head of Department
Assembling a protein transporter
How can you obtain high resolution structural information about protein complexes when you cannot determine the structure directly by techniques such as X-ray crystallography? This was the problem faced by Ben Berks' group in their work on the Tat protein transport system.
(Fig 1.) High precision evolutionary contacts between Tat proteins predict subunit packing interfaces. Reproduced from .
(Click to enlarge)
Bacteria use the Tat pathway to export folded proteins across their cell membrane. Tat transport is catalysed by three small membrane proteins called TatA, TatB, and TatC. During the transport cycle multiple copies of each of these proteins come together to transiently form the protein transporter . Berks and collaborators have previously determined the structures of the individual Tat components [2,3]. However, they did not know how these individual proteins assemble together in the translocation machine. Without this information it would be very difficult to understand how the transporter works. Unfortunately the Tat complexes are exceedingly challenging to work with and attempts to determine their structures by standard techniques have so far been unsuccessful. A novel approach was therefore required to determine the inter-protein contacts within the Tat apparatus.