Molecular Playground/ClyA: Difference between revisions
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[[Image:ClyA.png]] [[Image:ClyA-protomer.png]] | [[Image:ClyA.png]] [[Image: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. | 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. | ||
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. | |||
==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 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 the forces that influence polymer translocation through ClyA. | ||