Literature summary for 3.4.21.B57 extracted from

Foophow, T.; Tanaka, S.; Angkawidjaja, C.; Koga, Y.; Takano, K.; Kanaya, S.
Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability (2010), J. Mol. Biol., 400, 865-877.

Search for more literature for 3.4.21.B57

Cloned(Commentary)

Cloned (Comment)	Organism
Tk-S359A without N- and C-propeptides is overproduced in Escherichia coli in a soluble form	Thermococcus kodakarensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop, vapor-diffusion method at 20 °C, the crystal structure of the active-site mutant of the proenzyme lacking C-propeptide (ProN-Tk-S359A) is determined at 2.0 A resolution	Thermococcus kodakarensis

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a series of active-site mutants of with (Tk-S359A/C) and without (Tk-S359A/CDeltaJ) beta-jelly roll domain. Both Tk-S359C and Tk-S359CDeltaJ exhibit protease activities, indicating that the beta-jelly roll domain is not required for folding or activity. The Tm value of Tk-S359ADeltaJ determined by far-UV CD spectroscopy in the presence of 10-mM CaCl2 is lower than that of Tk-S359A by 29.4°C. The Tm value of Tk-S359A is decreased by 29.5 °C by the treatment with 10 mM ethylenediaminetetraacetic acid, indicating that the beta-jelly roll domain contributes to the stabilization of Tk-S359A only in a Ca2+-bound form	Thermococcus kodakarensis

General Stability

General Stability	Organism
the beta-jelly roll domain is required for hyperstabilization of the protein. This domain contains two Ca2+ ions and contributes to the stabilization of the protein only in a Ca2+-bound form	Thermococcus kodakarensis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	two Ca2+ ions bind to the beta-jelly roll domain	Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
42000	-	gel filtration	Thermococcus kodakarensis
44000	-	1 * 44000, mutant enzyme S359A, SDS-PAGE	Thermococcus kodakarensis

Organism

Organism	UniProt	Comment	Textmining
Thermococcus kodakarensis	P58502	sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106)	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the enzyme is autoprocessed from its precursor with N- and C-propeptides	Thermococcus kodakarensis

Subunits

Subunits	Comment	Organism
monomer	1 * 44000, mutant enzyme S359A, SDS-PAGE	Thermococcus kodakarensis

Synonyms

Synonyms	Comment	Organism
Tk-SP	-	Thermococcus kodakarensis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	attachment of a beta-jelly roll domain to the C-terminus is one of the strategies of the proteins from hyperthermophiles to adapt to high-temperature environment	Thermococcus kodakarensis
58.9	-	Tm value of a mutant enzyme without beta-jelly roll domain (Tk-S359A/CDeltaJ), 10 mM CaCl2	Thermococcus kodakarensis
88.3	-	Tm value of mutant enzyme S359A, 10 mM CaCl2	Thermococcus kodakarensis

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Release 2023.1 (January 2023)