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Literature summary for 1.8.4.2 extracted from
- Structural basis of a thiol-disulfide oxidoreductase in the hedgehog-forming actinobacterium Corynebacterium matruchotii (2018), J. Bacteriol., 200, e00783-17 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| DTT | at DTT concentrations of 5-10 mM Corynebacterium matruchotii doubling time increases more than 2.5-3fold, the enzyme mediates posttranslocational protein folding in Corynebacterium matruchotii | Corynebacterium matruchotii |  |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant enzyme MdbA, sitting drop vapor diffusion technique, a well solution containing 31.4% PEG 8000, 150 mM citrate buffer, pH 5.5 is used, 4-16 °C, 10 days, X-ray diffraction structure determination and analysis at 1.2 A, molecular replacement using the Corynebacterium diphtheriae MdbA structure (PDB ID 5C00) as the starting model | Corynebacterium matruchotii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C91A/C94A | site-directed mutagenesis, catalytically inactive mutant | Corynebacterium matruchotii |
| additional information | heterologous expression of MdbACm in the Corynebacterium diphtheriae DELTAmdbA mutant rescues its known defects in cell growth and morphology, toxin production, and pilus assembly, and this thiol-disulfide oxidoreductase activity requires the catalytic motif CXXC. MdbA gene deletion in Corynebacterium matruchotii by gene replacement method. The Corynebacterium diphtheriae DELTAmdbA mutant is able to grow only at 30°C. This defect is rescued by expression of MdbACd. Expression of MdbACm in this mutant also rescues the growth defect. Generation of a MdbA gene deletion mutant of Corynebacterium matruchotii by gene replacement method | Corynebacterium matruchotii |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | membrane-bound, the enzyme is a transmembrane protein | Corynebacterium matruchotii | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 glutathione + pilin FimA-disulfide | Corynebacterium matruchotii | - |
glutathione-disulfide + pilin FimA-dithiol | - |
? | |
| 2 glutathione + pilin FimA-disulfide | Corynebacterium matruchotii ATCC 14266 | - |
glutathione-disulfide + pilin FimA-dithiol | - |
? | |
| 2 glutathione + protein-disulfide | Corynebacterium matruchotii | - |
glutathione-disulfide + protein-dithiol | - |
? | |
| 2 glutathione + protein-disulfide | Corynebacterium matruchotii ATCC 14266 | - |
glutathione-disulfide + protein-dithiol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium matruchotii | - |
- |
- |
| Corynebacterium matruchotii ATCC 14266 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 glutathione + pilin FimA-disulfide | - |
Corynebacterium matruchotii | glutathione-disulfide + pilin FimA-dithiol | - |
? | |
| 2 glutathione + pilin FimA-disulfide | recombinant FimA expressed in Escherichia coli | Corynebacterium matruchotii | glutathione-disulfide + pilin FimA-dithiol | - |
? | |
| 2 glutathione + pilin FimA-disulfide | - |
Corynebacterium matruchotii ATCC 14266 | glutathione-disulfide + pilin FimA-dithiol | - |
? | |
| 2 glutathione + pilin FimA-disulfide | recombinant FimA expressed in Escherichia coli | Corynebacterium matruchotii ATCC 14266 | glutathione-disulfide + pilin FimA-dithiol | - |
? | |
| 2 glutathione + protein-disulfide | - |
Corynebacterium matruchotii | glutathione-disulfide + protein-dithiol | - |
? | |
| 2 glutathione + protein-disulfide | - |
Corynebacterium matruchotii ATCC 14266 | glutathione-disulfide + protein-dithiol | - |
? | |
| additional information | MdbACm directly catalyzes disulfide bond formation in proteins in vitro | Corynebacterium matruchotii | ? | - |
- |
|
| additional information | MdbACm directly catalyzes disulfide bond formation in proteins in vitro | Corynebacterium matruchotii ATCC 14266 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 26800, SDS-PAGE | Corynebacterium matruchotii |
| More | the enzyme structure of MdbACm possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-like fold and an extended alpha-helical domain. The MdbA alpha-helical domain comprises 7 alpha-helices | Corynebacterium matruchotii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MdbA | - |
Corynebacterium matruchotii |
| MdbACm | - |
Corynebacterium matruchotii |
| thiol-disulfide oxidoreductase | - |
Corynebacterium matruchotii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Corynebacterium matruchotii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3 | - |
assay at | Corynebacterium matruchotii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the oxidoreductase MdbA identified from Corynebacterium matruchotii is highly homologous to the Corynebacterium diphtheriae thiol-disulfide oxidoreductase MdbA (MdbACd). The disulfide oxidoreductase activity requires the catalytic motif CXXC. MdbACm is a major thiol-disulfide oxidoreductase, which likely mediates posttranslocational protein folding in Corynebacterium matruchotii by a mechanism that is conserved in Actinobacteria, the enzyme is essential in the organism. Corynebacterium matruchotii MdbA can replace Corynebacterium diphtheriae MdbA in mutants to maintain normal cell growth and morphology, toxin production, and pilus assembly. The protein active site closely resembles active sites of other MdbA/DsbA enzymes. The superposition of Corynebacterium matruchotii and Corynebacterium diphtheriae MdbA active sites does not show notable changes of active-site arrangement, overview | Corynebacterium matruchotii |
| metabolism | the actinobacterium Corynebacterium matruchotii has been implicated in nucleation of oral microbial consortia leading to biofilm formation | Corynebacterium matruchotii |
| additional information | the enzyme structure of MdbACm possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-like fold and an extended alpha-helical domain. The MdbA alpha-helical domain comprises 7 alpha-helices. The conserved catalytic CHYC motif (residues 91 to 94) forms the active site together with a conserved cis-Pro loop (residues S221 and P222). Structure modeling and structure comparisons, overview | Corynebacterium matruchotii |
| physiological function | the organism encodes a large number of exported proteins containing paired cysteine residues. Proteins possessing 2 or more cysteine residues made up 58.4% of the Corynabacterium matruchotii proteome (1530 of 2619 proteins). In the Gram-positive actinobacteria, oxidative protein folding via disulfide bond formation appears to be the major pathway for posttranslocational folding of these unfolded proteins. The oxidoreductase MdbA identified from Corynebacterium matruchotii, MdbACm, catalyzes disulfide bond formation within the actinobacterial pilin FimA | Corynebacterium matruchotii |
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