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Literature summary for 7.3.2.6 extracted from

  • Bevers, L.E.; Schwarz, G.; Hagen, W.R.
    A molecular basis for tungstate selectivity in prokaryotic ABC transport systems (2011), J. Bacteriol., 193, 4999-5001.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.3.2.6

Cloned(Commentary)

Cloned (Comment) Organism
expression in TOP10 cell Escherichia coli
expression in TOP10 cell Pyrococcus furiosus

Protein Variants

Protein Variants Comment Organism
D160A mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant is no longer able to selectively bind tungstate Pyrococcus furiosus
D160N mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant is no longer able to selectively bind tungstate Pyrococcus furiosus
E218A mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant retains specificity for tungstate and displays presence of two binding sites with different affinities Pyrococcus furiosus
E218Q mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant retains specificity for tungstate Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Pyrococcus furiosus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ModA is able to bind both tungstate and molybdate with very high affinities but is unable to replace one oxoanion with the other in a displacement titration Escherichia coli ?
-
 ?
additional information the octahedral W(VI)/Mo(VI)-binding motif present in WtpA proteins is essential for its displayed binding preference for tungstate over molybdate Pyrococcus furiosus ?
-
 ?

Synonyms

Synonyms Comment Organism
ModA
-
 Escherichia coli
WtpA
-
 Pyrococcus furiosus