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Literature summary extracted from

  • Johs, A.; Harwood, I.M.; Parks, J.M.; Nauss, R.E.; Smith, J.C.; Liang, L.; Miller, S.M.
    Structural characterization of intramolecular Hg2+ transfer between flexibly linked domains of mercuric ion reductase (2011), J. Mol. Biol., 413, 639-656.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.16.1.1 gene merA, expression as wild-type and mutant N-terminally His6-tagged and maltose-binding protein fusion proteins with a 3C protease cleavage site in Escherichia coli strain TOP10 and C43 Shigella flexneri

Protein Variants

EC Number Protein Variants Comment Organism
1.16.1.1 C135A site-directed mutagenesis Shigella flexneri
1.16.1.1 C140A site-directed mutagenesis Shigella flexneri
1.16.1.1 C14A site-directed mutagenesis Shigella flexneri
1.16.1.1 C561A site-directed mutagenesis Shigella flexneri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.16.1.1 Hg + NADP+ + H+ Shigella flexneri
-
 Hg2+ + NADPH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.16.1.1 Shigella flexneri
-
 gene merA from the Tn21 mer operon
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.16.1.1 recombinant wild-type and mutant N-terminally His6-tagged and maltose-binding protein fusion enzymes from Escherichia coli strain C43 by amylose affinity chromatography, cleavage of the tags by 3C protease, ultrafiltration, and gel filtration Shigella flexneri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.1.1 Hg + NADP+ + H+
-
 Shigella flexneri Hg2+ + NADPH
-
 r

Subunits

EC Number Subunits Comment Organism
1.16.1.1 homodimer structure homology modelling, overview Shigella flexneri

Synonyms

EC Number Synonyms Comment Organism
1.16.1.1 MerA
-
 Shigella flexneri

Cofactor

EC Number Cofactor Comment Organism Structure
1.16.1.1 FAD one FAD bound to each MerA catalytic core monomer Shigella flexneri
1.16.1.1 NADP+
-
 Shigella flexneri
1.16.1.1 NADPH
-
 Shigella flexneri

General Information

EC Number General Information Comment Organism
1.16.1.1 additional information many MerA proteins possess metallochaperone-like N-terminal domains (NmerA) that can transfer Hg2+ to the catalytic core domain (Core) for reduction to Hg0. These domains are tethered to the homodimeric core by an about 30-residue linkers that are susceptible to proteolysis, interactions of NmerA and the Core in the full-length protein, structure homology modelling amd structure-function analysis, detailed overview. Binding of Hg2+ to MerA does not alter its hydrodynamic volume Shigella flexneri