Cryo-electron microscopy has become a powerful new structural technique to obtain atomic resolution structures of membrane proteins. By combining the experimental structures with molecular dynamics simulations of the protein in a realistic environment including a membrane and solvent (water and ions), new insights regarding the protein function can be obtained that are not available from a single technique alone.
NHE9 is a sodium/proton exchanger in mammals, part of a large family of secondary active transporters. Our collaborators (David Drew at the University of Stockholm) solved the structure of NHE9 (SLC9A9) from horse with cryo electron-microscopy to 3.2 Å resolution in an inward facing conformation, the first structure of a mammalian sodium/proton antiporter. Functional measurements, structural bioinformatics, and MD simulations all indicate that many components of the transport mechanism are similar between prokaryotic and mammalian sodium/proton antiporters.
Dr. E. J. Norminton on
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