Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability.

Abstract

Tk-SP is a hyperthermostable subtilisin-like serine protease from Thermococcus kodakaraensis and is autoprocessed from its precursor (Pro-Tk-SP) with N- and C-propeptides. The crystal structure of the active-site mutant of Pro-Tk-SP lacking C-propeptide, ProN-Tk-S359A, was determined at 2.0 A resolution. ProN-Tk-S359A consists of the N-propeptide… (More)
DOI: 10.1016/j.jmb.2010.05.064

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Cite this paper

@article{Foophow2010CrystalSO, title={Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability.}, author={Tita Foophow and Shun-ichi Tanaka and Clement Angkawidjaja and Yuichi Koga and Kazufumi Takano and Shigenori Kanaya}, journal={Journal of molecular biology}, year={2010}, volume={400 4}, pages={865-77} }