Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints
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Bacteria that survive in mercury-polluted environments contain an operon whose proteins constitute a mercury detoxification system (Barkay et al. 2003) that functions by importing highly toxic Hg(II) into the cytoplasm of the bacterial cell and enzymatically transforming it to its less toxic and volatile form Hg(0), which is passively eliminated. Initially, Hg(II) binds to the periplasmic protein MerP, which delivers it to a membrane protein transporter such as MerF. The membrane protein is responsible for transporting Hg(II) across the cell membrane and delivering it to MerA, the cytoplasmic mercuric reductase, a multi-domain enzyme that reduces Hg(II) to Hg(0). Understanding the molecular mechanism of mercury detoxification is important for both environmental and biomedical applications of components of the bacterial mercury detoxification system. Atomic resolution structures of MerP and MerA have been determined (Schiering et al. 1991; Steele and Opella 1997)....
KeywordsPhospholipid Bilayer Magic Angle Spin Chemical Shift Anisotropy Atom RMSD Torsion Angle Dynamic
This research was supported by grants from R01GM099986, P41EB002031, R01EB005161, R01GM066978, R01GM100265 and P01AI074805 from the National Institutes of Health. It utilized the BTRC for NMR Molecular Imaging of Proteins at UCSD.