Proteus mirabilis copper resistance protein is a shape-shifting redox foldase
Status: This talk is in preparation - details may change
In the hunt for targets for a new class of antibacterials to overcome antibiotic resistance, we stumbled across an extraordinary shape-shifting protein. Proteus mirabilis ScsC – which supports bacterial swarming motility under copper stress – is a disulfide isomerase. Previously characterised bacterial disulfide isomerases are dimeric quality control agents that shuffle incorrect disulfide bonds in misfolded proteins. Unexpectedly, we show that PmScsC is not a dimer – but a trimer. We solved three crystal structures of PmScsC, revealing that it undergoes extraordinary twisting and extending motions. These motions – that underpin the function of PmScsC – are a consequence of a short, highly flexible shape-shifting motif resulting in major changes to the overall dimensions of the proteins, almost doubling its length in one dimension.
Date: 8 June 2016, 12:00 (Wednesday, 7th week, Trinity 2016)
Venue: Wellcome Trust Centre for Human Genetics, Headington OX3 7BN
Venue Details: Meeting Room A/B
Speaker: Prof Jennifer Martin (The University of Queensland in Australia)
Organising department: Wellcome Trust Centre for Human Genetics
Organiser: Agata Krupa (Wellcome Trust Centre for Human Genetics)
Organiser contact email address:
Host: Prof E.Yvonne Jones (University of Oxford)
Part of: Strubi seminars
Booking required?: Not required
Audience: Members of the University only
Editor: Agata Krupa