Abstract
A general NMR method for determining the three-dimensional structures of membrane proteins in phospholipid bilayers is illustrated with the backbone structure of the mercury transporter MerF from the bacterial mercury detoxification system. MerF has two hydrophobic trans membrane helices and is responsible for the transport of mercuric ions and methylmercury across the membrane, from MerP in the periplasm to MerA in the cytoplasm. MerA is mercuric reductase, the enzyme that reduces the toxic Hg(II) to Hg(0). The structure determination method applied to membrane proteins combines Oriented Sample (OS) solid-state NMR and Magic Angle Spinning (MAS) solid-state NMR methods to measure angular constraints for structure calculations. The three-dimensional protein structure determined in its native bilayer environment enables the interactions of the mercury-binding cysteines with the metal ions and other proteins to be described.
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