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Literature summary for 1.16.1.1 extracted from

  • Hong, L.; Sharp, M.A.; Poblete, S.; Biehl, R.; Zamponi, M.; Szekely, N.; Appavou, M.S.; Winkler, R.G.; Nauss, R.E.; Johs, A.; Parks, J.M.; Yi, Z.; Cheng, X.; Liang, L.; Ohl, M.; Miller, S.M.; Richter, D.; Gompper, G.; Smith, J.C.
    Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase (2014), Biophys. J., 107, 393-400 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli strain BL21(DE3) pLysS Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Hg2+ + NADPH Pseudomonas aeruginosa
-
 Hg + NADP+ + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Hg + NADP+ + H+ = Hg2+ + NADPH MerA possesses metallochaperone-like N-terminal domains (NmerA) tethered to its catalytic core domain by linkers. The NmerA domains interacts principally through electrostatic interactions with the core, leashed by the linkers so as to subdiffuse on the surface over an area close to the core C-terminal Hg(II)-binding cysteines Pseudomonas aeruginosa
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hg2+ + NADPH
-
 Pseudomonas aeruginosa Hg + NADP+ + H+
-
 ?

Subunits

Subunits Comment Organism
dimer interdomain dynamics in MerA, overview Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
MerA
-
 Pseudomonas aeruginosa
mercuric ion reductase
-
 Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Pseudomonas aeruginosa
NADPH
-
 Pseudomonas aeruginosa

General Information

General Information Comment Organism
additional information full-length MerA homodimer structure and transfer of Hg(II) from the solvent into the catalytic sites of the MerA core, overview. Enzyme structure-function analysis by molecular dynamics, coarse-grained simulations, small-angle neutron scattering, neutron spin-echo spectroscopy, and dynamic light scattering Pseudomonas aeruginosa