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FEBS Lett. 2008 Nov 26;582(28):3875-8. doi: 10.1016/j.febslet.2008.10.025. Epub 2008 Oct 23.

Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding.

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1
Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.

Abstract

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.

PMID:
18951896
DOI:
10.1016/j.febslet.2008.10.025
[Indexed for MEDLINE]
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