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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
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:
jones-pa@strubi.ox.ac.uk
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
