Molecular Playground/ClyA: Difference between revisions

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Bib Yang, Monifa Fahie, Michal Harel

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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' />
 ==About this Structure==
-[[Image:ClyA-monomer2.png]]
-Figure 1. The soluble ClyA monomer, [[1QOY]], rendered in PyMol.
 [[1QOY]] in Figure 1 above 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.
-Its crystal structure, [[2WCD]], as shown in Figure 2 below, 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.
-[[Image:ClyA.png]] [[Image:ClyA-protomer.png]]
+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.
-Figure 2. The dodecameric ClyA crystal structure revealing its lumen (left), rendered in PyMol.  The protomer of ClyA is on the right.
-The protomer of ClyA, shown in Figure 2 on the right, 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.
 <scene name='57/571278/Clya_oligomer/1'>The oligomeric form of ClyA</scene>