Crystallization (Comment) | Organism |
---|---|
sitting-drop vapour-diffusion method at 4°C. The crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin), which is refolded in the presence of Ca2+ and absence of Tk-propeptide, is determined at 2.16 A resolution. This structure is the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin | Thermococcus kodakarensis |
Protein Variants | Comment | Organism |
---|---|---|
S324A | the crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin), which is refolded in the presence of Ca2+ and absence of Tk-propeptide, is determined at 2.16 A resolution. This structure is the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin. The counting of amino acids refers to the enzyme protein without the signal peptide (amino acid 1-24) and the propeptide (amino acid 25-106) | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | P58502 | sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106) | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | Tk-subtilisin is matured from Pro-Tk-subtilisin upon autoprocessing and degradation of Tk-propeptide. Tk-subtilisin does not require Tk-propeptide for folding but requires it for acceleration of folding | Thermococcus kodakarensis |
Synonyms | Comment | Organism |
---|---|---|
Tk-subtilisin | - |
Thermococcus kodakarensis |