Structural Research of Bacterial Mercury Detoxification Proteins

Mercury (Hg) is a toxic heavy metal that poses a significant threat to human health and the environment. Bacteria have evolved a variety of mechanisms to detoxify Hg, including the expression of specific proteins that bind and sequester Hg ions. Structural research on these bacterial Hg detoxification proteins is crucial for understanding their mechanisms of action and developing new strategies for the remediation of Hg-contaminated sites.

In the bacterial mercury detoxification system, Hg (II) is transported across the intracellular membrane into the cytoplasm by membrane proteins such as MerF. With both metal transfer and transport activities, the structural biology of MerF is too complex to be explained simply by the binding of Hg (II) to cysteine pairs. Therefore, it is necessary to determine the three-dimensional structure in which it performs its function in the phospholipid bilayer. MerFt is the 60-residue helix-loop-helix integral membrane core of MerF. Some researchers have studied the three-dimensional structure of MerFt in proteoliposomes by using the NMR method.

Figure 1. Structure of MerFt in DMPC phospholipid bilayers. (Das B B, et al., 2012)

Table 1. Structural Research of Bacterial Mercury Detoxification Proteins.

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References

1. De Angelis A A, et al. Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy. Journal of the American Chemical Society. 2006, 128(37): 12256-12267.
2. Howell S C, et al. NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system. Biochemistry. 2005, 44(13): 5196-5206.
3. Das B B, et al. Structure determination of a membrane protein in proteoliposomes. Journal of the American Chemical Society. 2012, 134(4): 2047-2056.