Literature summary for 1.16.1.1 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.

Search for more literature for 1.16.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
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)

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

Subunits

Subunits	Comment	Organism
homodimer	structure homology modelling, overview	Shigella flexneri

Synonyms

Synonyms	Comment	Organism
MerA	-	Shigella flexneri

Cofactor

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

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)