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Literature summary for 3.4.22.71 extracted from
- X-ray structure of Clostridium perfringens sortase B cysteine transpeptidase (2017), Biochem. Biophys. Res. Commun., 493, 1267-1272 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Clostridium perfringens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structures of SrtB and its inactive mutant at 2.2 A and 1.8 A, respectively. The position of Cys232 found is preferable for the catalytic reaction to occur. Structural comparison with other class B sortases demonstrates that the catalytic site likely converts between two forms. The movement of Cys232 between the two forms may help His136 deprotonate Cys232 to be activated as a thiolate | Clostridium perfringens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C232S | inactive | Clostridium perfringens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium perfringens | Q8XN25 | - |
- |
| Clostridium perfringens 13 | Q8XN25 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CPE0513 | - |
Clostridium perfringens |
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Release 2023.1 (January 2023)
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