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Is the cytoplasmic loop of MerT, the mercuric ion transport protein, involved in mercury transfer to the mercuric reductase?
Author(s) -
Rossy Emmanuel,
Sénèque Olivier,
Lascoux David,
Lemaire David,
Crouzy Serge,
Delangle Pascale,
Covès Jacques
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.041
Subject(s) - periplasmic space , cysteine , mercury (programming language) , chemistry , cytoplasm , stereochemistry , amino acid , nuclear magnetic resonance spectroscopy , biochemistry , biophysics , crystallography , enzyme , biology , escherichia coli , computer science , programming language , gene
In MerT, the mercury transporter, a first cysteine pair, located in the first trans ‐membrane helix, receives mercury from the periplasm. Then, a second cysteine pair, housed in a cytoplasmic loop connecting the second and the third trans ‐membrane helices, is thought to transfer the metal to another cysteine pair located in the N‐terminal extension of the mercuric reductase. We found that a 23‐amino acid synthetic peptide corresponding to the cytoplasmic loop can bind one mercury atom per molecule and that this mercury atom can be transferred specifically to MerAa. The solution structure of Hg‐bound ppMerT has been solved by 1 H NMR spectroscopy.