Molecular Playground/ClyA: Difference between revisions
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[[Image:ClyA-monomer2.png]] | [[Image:ClyA-monomer2.png]] | ||
[[1QOY]] is a monomer from the dodecameric pore-forming toxin from [http://en.wikipedia.org/wiki/Escherichia_coli ''Escherichia coli'']. It is comprised of four alpha helicies | [[1QOY]] is a monomer from the dodecameric pore-forming toxin (PFT) from [http://en.wikipedia.org/wiki/Escherichia_coli ''Escherichia coli'']. It is 34kDa protein comprised of four alpha helicies, a smaller fifth alpha helix, and a beta tongue. | ||
Though its crystal structure,[[2WCD]] revealed a dodecamer, larger [http://pubs.acs.org/doi/abs/10.1021/ja4053398 pores] have been isolated, as well. | Though its crystal structure,[[2WCD]] revealed a dodecamer, larger [http://pubs.acs.org/doi/abs/10.1021/ja4053398 pores] have been isolated, as well. | ||
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==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. | 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 the forces that influence polymer translocation through ClyA. | ||
Revision as of 11:47, 27 March 2014
<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 34kDa protein comprised of four alpha helicies, a smaller fifth alpha helix, and a beta tongue. Though its crystal structure,2WCD revealed a dodecamer, larger pores have been isolated, as well.
File:ClyA.png File:ClyA-protomer.png
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.