“Structure and Mechanism of a Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer”
Prof. Ming Tang
College of Staten Island CUNY
The integral membrane protein DsbB in Escherichia coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins. We have developed a high-resolution structural model by combining experimental X-ray and solid-state NMR with molecular dynamics (MD) simulations. We embedded the high-resolution DsbB structure, derived from the joint calculation with X-ray reflections and solid-state NMR restraints, into the lipid bilayer and performed MD simulations to provide a mechanistic view of DsbB function in the membrane. Further, we revealed the membrane topology of DsbB by selective proton spin diffusion experiments, which directly probe the correlations of DsbB with water and lipid acyl chains. NMR data also support the model of a flexible periplasmic loop and an interhelical hydrogen bond between Glu26 and Tyr153. Significant sensitivity enhancement of membrane protein was achieved using chelator lipids with paramagnetic metal ions, which can be readily incorporated into the existing preparation of membrane samples. These solid-state NMR techniques are transferrable to many membrane-associated protein systems.
6:00 pm Dinner
7:00 pm Seminar
A57, Frick Chemistry Laboratory Atrium, Princeton University
$15 employed / $5 students, postdoc, retired, unemployed.
No charge for seminar only.
Directions to Frick Chemistry Laboratory