Journal
FEBS LETTERS
Volume 582, Issue 28, Pages 3875-3878Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.10.025
Keywords
Subtilisin; Crystal structure; Propeptide; Folding; Thermococcus kodakaraensis
Funding
- Japan Synchrotron Radiation Research Institute [2008A1106]
- Industrial Technology Research Grant Program
- New Energy and Industrial Technology Development Organization (NEDO) of Japan
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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 Ca(2+) and absence of Tk-propeptide, was determined at 2.16 angstrom resolution. This structure is essentially the same as that of Tk-subtilisin matured from Pro-Tksubtilisin. S324A-subtilisin* was refolded with a rate constant of 0.17 and 1.8 min(-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. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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