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]
Producer: 20090717Description: 229-40 p. digitalISSN:- 1399-0047
- 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
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
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