Structures of the Reduced and Mercury-Bound Forms of MerP, the Periplasmic Protein from the Bacterial Mercury Detoxification System

• Published in: Biochemistry (Easton) 1997-06, Vol.36 (23), p.6885-6895
• Main Authors: Steele, Ruth A, Opella, Stanley J
• Format: Article
• Language: English
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Carrier Proteins - chemistry; Carrier Proteins - metabolism; Escherichia coli; Magnetic Resonance Spectroscopy; Mercury - chemistry; Mercury - metabolism; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Protein Conformation; Protein Folding; Protein Structure, Secondary; Proteins; Shigella flexneri; Software; Solutions
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi9631632

Bacteria carrying plasmids with the mer operon, which encodes the proteins responsible for the bacterial mercury detoxification system, have the ability to transport Hg(II) across the cell membrane into the cytoplasm where it is reduced to Hg(0). This is significant because metallic mercury is relatively nontoxic and volatile and thus can be passively eliminated. The structures of the reduced and mercury-bound forms of merP, the periplasmic protein, which binds Hg(II) and transfers it to the membrane transport protein merT, have been determined in aqueous solution by multidimensional NMR spectroscopy. The 72-residue merP protein has a βαββαβ fold with the two α helices overlaying a four-strand antiparallel β sheet. Structural differences between the reduced and mercury-bound forms of merP are localized to the metal binding loop containing the consensus sequence GMTCXXC. The structure of the mercury-bound form of merP shows that Hg(II) is bicoordinate with the Cys side chain ligands, and this is confirmed by the chemical shift frequency of the 199Hg resonance.