Molecular Playground/ClyA
<Structure load='1qoy' size='350' frame='true' align='left' caption='ClyA monomer in its inactive form' scene='<scene name='57/571278/Clya_monomer/1'>
About this StructureAbout this Structure
1QOY is a monomer from the dodecameric pore-forming toxin (PFT) from Escherichia coli. It is a 34kDa protein comprised of four alpha helicies, a smaller fifth alpha helix, and a beta tongue. ClyA has been shown to form pores through a non-classical assembly pathway, excreted in oligomeric form in outer-membrane vesicles (OMV) as pre-pores. Only until ClyA reaches the target host membrane does it form the dodecameric PFT with hemolytic activity. Though its crystal structure,2WCD revealed a dodecamer, larger pores have been isolated, as well.
Research on ClyA at UMass AmherstResearch on ClyA at UMass Amherst
The Chen Lab, in collaboration with the Heuck lab, recently published a paper on ClyA assembly. Currently, we are investigating the forces that influence polymer translocation through ClyA.