Difference between revisions of "Part:BBa K1420003"
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merP is in charge of periplasmic transportation of mercury. This protein has two conserved cysteine residues for specific binding with the mercury ion, Hg(II). | merP is in charge of periplasmic transportation of mercury. This protein has two conserved cysteine residues for specific binding with the mercury ion, Hg(II). | ||
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MerP is a 72 amino acid periplasmic membrane protein. The merP protein functions as a monomer, binding a single Hg(II) ion at the two conserved cysteine residues. These Cysteine's define the metal binding motif of PerP. Similar motifs are also found in other proteins that are involved in the transportation of thiophilic metal cations. MerP is not essential for Hg(II) uptake, as MerT can also do much of the same work. However, there is the possibility of a Cysteine mutation on MerT which blocks Hg(II) uptake, and this mutation cannot be found on MerP, making it a redundant periplasmic transporter. | MerP is a 72 amino acid periplasmic membrane protein. The merP protein functions as a monomer, binding a single Hg(II) ion at the two conserved cysteine residues. These Cysteine's define the metal binding motif of PerP. Similar motifs are also found in other proteins that are involved in the transportation of thiophilic metal cations. MerP is not essential for Hg(II) uptake, as MerT can also do much of the same work. However, there is the possibility of a Cysteine mutation on MerT which blocks Hg(II) uptake, and this mutation cannot be found on MerP, making it a redundant periplasmic transporter. | ||
Revision as of 23:09, 9 October 2014
MerP, mercuric transport protein periplasmic component
merP is in charge of periplasmic transportation of mercury. This protein has two conserved cysteine residues for specific binding with the mercury ion, Hg(II).
MerP is a 72 amino acid periplasmic membrane protein. The merP protein functions as a monomer, binding a single Hg(II) ion at the two conserved cysteine residues. These Cysteine's define the metal binding motif of PerP. Similar motifs are also found in other proteins that are involved in the transportation of thiophilic metal cations. MerP is not essential for Hg(II) uptake, as MerT can also do much of the same work. However, there is the possibility of a Cysteine mutation on MerT which blocks Hg(II) uptake, and this mutation cannot be found on MerP, making it a redundant periplasmic transporter.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]