The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.

Carius, Yvonne

The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation. [electronic resource] - Acta crystallographica. Section D, Biological crystallography Mar 2009 - 229-40 p. digital

Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't

1399-0047

10.1107/S0907444908043023 doi


Amino Acid Motifs
Amino Acid Sequence
Bacterial Proteins--chemistry
Binding Sites
Crystallography, X-Ray
Dimerization
Disulfides--metabolism
Glutaredoxins--chemistry
Models, Molecular
Molecular Sequence Data
Oxidation-Reduction
Oxidoreductases Acting on Sulfur Group Donors--metabolism
Paracoccus pantotrophus--enzymology
Protein Conformation
Protein Disulfide Reductase (Glutathione)--chemistry
Recombinant Fusion Proteins--chemistry
Selenomethionine--chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Structure-Activity Relationship
Sulfur--metabolism
Thioredoxins--chemistry