Structural highlights
Function
[TKSU_THEKO] Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Tk-subtilisin (a subtilisin homologue from Thermococcus kodakaraensis) is matured from Pro-Tk-subtilisin upon autoprocessing and degradation of Tk-propeptide. To analyze the folding mechanism of Tk-subtilisin, the crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin*), which was refolded in the presence of Ca2+ and absence of Tk-propeptide, was determined at 2.16A resolution. This structure is essentially the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin. S324A-subtilisin* was refolded with a rate constant of 0.17 and 1.8min(-1) at 30 degrees C in the absence and presence of Tk-propeptide, respectively, indicating that Tk-subtilisin does not require Tk-propeptide for folding but requires it for acceleration of folding.
Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding.,Tanaka S, Takeuchi Y, Matsumura H, Koga Y, Takano K, Kanaya S FEBS Lett. 2008 Nov 26;582(28):3875-8. Epub 2008 Oct 23. PMID:18951896[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tanaka S, Takeuchi Y, Matsumura H, Koga Y, Takano K, Kanaya S. Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding. FEBS Lett. 2008 Nov 26;582(28):3875-8. Epub 2008 Oct 23. PMID:18951896 doi:10.1016/j.febslet.2008.10.025
