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
Figure 1. The soluble ClyA monomer. 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.
File:ClyA.png File:ClyA-protomer.png Figure 2. The dodecameric ClyA crystal structure rendered in PyMol (left), revealing the lumen of the pore. The protomer of ClyA is on the right.
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.