Description
The bacterial magnesium transporter CorA from Thermotoga maritima has been studied with small angle neutron scattering in match out deuterated DDM micelles. From recent cryoEM data and crystal structures, the membrane protein is expected to undergo a large conformational change upon magnesium binding, where its five subunits make a more compact and symmetric structure compared to the unbound state. In our experiment, we were not able to observe a conformational change, which opens questions about the solution properties of CorA. In our ongoing studies, we investigate structure and function of CorA in H2O and D2O based solvents combining small angle scattering with other biophysical methods.
Primary author
Mr
Tidemand Johansen Nicolai
(Niels Bohr Institute, University of Copenhagen)
