Molecular Playground/ClyA: Difference between revisions
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<scene name='57/571278/Clya_monomer/2'>ClyA monomer in its inactive form</scene> | <scene name='57/571278/Clya_monomer/2'>ClyA monomer in its inactive form</scene> | ||
[[1QOY]] is a monomer from the dodecameric pore-forming toxin (PFT) from [http://en.wikipedia.org/wiki/Escherichia_coli ''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. | [[1QOY]] is a monomer from the dodecameric pore-forming toxin (PFT) from [http://en.wikipedia.org/wiki/Escherichia_coli ''Escherichia coli'']. It is a 34kDa protein comprised of four alpha helicies, a smaller fifth alpha helix, and a <font color="purple">beta tongue</font>. 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. | ||
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<scene name='57/571278/Clya_protomer/1'>ClyA protomer</scene> | <scene name='57/571278/Clya_protomer/1'>ClyA protomer</scene> | ||
Revision as of 18:21, 13 May 2014
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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.
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The protomer of ClyA reveals slight differences between the monomer and protomer (from the dodecamer). The major conformational changes between the monomer and the protomer are the positions of the N-terminal helix and the beta-tongue. As ClyA oligomerizes and forms a pore, the N-terminal helix swings to the opposite side of the molecule while the beta-tongue changes its conformation and turns into an alpha-helix that interacts with the lipid bilayer.
Its crystal structure, 2WCD, reveals 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 electroosmotic flow and electrophoretic force, the forces that influence polymer translocation through ClyA.