1AFI

STRUCTURE OF THE REDUCED FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES

Summary for 1AFI

• Entry DOI: 10.2210/pdb1afi/pdb
• Descriptor: MERP (1 entity in total)
• Functional Keywords: mercury detoxification, periplasmic, heavy metal transport, alpha-beta sandwich
• Biological source: Shigella flexneri
• Cellular location: Periplasm (Probable): P04129
• Total number of polymer chains: 1
• Total formula weight: 7483.63

Authors

Steele, R.A.,Opella, S.J. (deposition date: 1997-03-07, release date: 1997-07-23, Last modification date: 2024-05-22)

Primary citation

Steele, R.A.,Opella, S.J.
Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system.
Biochemistry, 36:6885-6895, 1997

PubMed Abstract: 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 betaalpha betabeta alphabeta fold with the two alpha helices overlaying a four-strand antiparallel beta 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.

PubMed: 9188683
DOI: 10.1021/bi9631632

Experimental method

SOLUTION NMR