Molecular Playground/ClyA: Difference between revisions
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<Structure load='1QOY' size='350' frame='true' align='right' caption='ClyA monomer in its inactive form' scene='Insert optional scene name here' /> | <Structure load='1QOY' size='350' frame='true' align='right' caption='ClyA monomer in its inactive form' scene='Insert optional scene name here' /> | ||
==About this Structure== | ==About this Structure== | ||
<scene name='57/571278/Clya_monomer/2'>TextToBeDisplayed</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. | |||
<scene name='57/571278/Clya_oligomer/1'>The oligomeric form of ClyA</scene> | |||
Its crystal structure, [[2WCD]], reveals a dodecamer. Larger [http://pubs.acs.org/doi/abs/10.1021/ja4053398 pores] have been isolated, as well. | Its crystal structure, [[2WCD]], reveals a dodecamer. Larger [http://pubs.acs.org/doi/abs/10.1021/ja4053398 pores] have been isolated, as well. | ||
The protomer of ClyA reveals slight differences between the monomer and protomer. 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. | The protomer of ClyA reveals slight differences between the monomer and protomer. 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. | ||
==Research on ClyA at UMass Amherst== | ==Research on ClyA at UMass Amherst== | ||
The Chen Lab, in collaboration with the Heuck lab, recently published a paper on [http://www.jbc.org/content/288/43/31042.short, ClyA] assembly. Currently, we are investigating electroosmotic flow and electrophoretic force, the forces that influence polymer translocation through ClyA. | The Chen Lab, in collaboration with the Heuck lab, recently published a paper on [http://www.jbc.org/content/288/43/31042.short, ClyA] assembly. Currently, we are investigating electroosmotic flow and electrophoretic force, the forces that influence polymer translocation through ClyA. | ||
Revision as of 18:03, 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.
Its crystal structure, 2WCD, reveals a dodecamer. Larger pores have been isolated, as well.
The protomer of ClyA reveals slight differences between the monomer and protomer. 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.
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.