Literature summary for 3.4.21.62 extracted from

Tanaka, S.; Saito, K.; Chon, H.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon (2006), Acta Crystallogr. Sect. F, 62, 902-905.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of pro-S255A by pET25b in Escherichia coli BL21-Codon-Plus(DE3)	Thermococcus kodakarensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
pro-S255A crystallized in complex with Ca2+, by sitting-drop vapour-diffusion method, to 2.3 A resolution. Crystal belongs to space group I222, with unit cell parameters a = 92.69, b = 121.78, c = 77.53 A. Matthews coefficient is 2.6 A 3 Da-1 and the solvent content is 53.1%.	Thermococcus kodakarensis

Protein Variants

Protein Variants	Comment	Organism
S255A	active-site mutant of pro-subtilisin. Accumulates in cells in inclusion bodies like pro-subtilisin	Thermococcus kodakarensis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	six calcium ions bind to pro-S255A at the loop regions. The at least six Ca2+ ions bind to pro-S255A too tightly to be removed by dialysis	Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
45000	-	pro-S255A, gel filtration	Thermococcus kodakarensis

Organism

Organism	UniProt	Comment	Textmining
Thermococcus kodakarensis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
pro-S255A purified in the presence of 8 M urea. Refolded by removing urea in the presence of Ca2+. Further purified by gel filtration	Thermococcus kodakarensis

Subunits

Subunits	Comment	Organism
monomer	pro-S255A, SDSPAGE	Thermococcus kodakarensis

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Release 2023.1 (January 2023)