Literature summary for 3.4.19.1 extracted from

Menyhard, D.K.; Kiss-Szeman A.; Tichy-Racs, E.; Hornung, B.; Radi, K.; Szeltner, Z.; Domokos, K., Szamosi, I.; Naray-Szabo, G.; Polgar, L.; Harmat, V.
A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization (2013), J. Biol. Chem., 288, 17884-17894.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals are grown at 20°C by the hanging drop method	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O58323	-	-
Pyrococcus horikoshii DSM 12428	O58323	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pyrococcus horikoshii

Subunits

Subunits	Comment	Organism
hexamer	hexamers in the crystalline state are formed as trimers of dimers of the monomer enzyme. It is proposed that the mode of multimerization and self-assembly among oligopeptidases is finetuned by a shielding intent of a sticky-edge, insertions, and N- and C-terminal extensions, whereas to maintain the effectiveness of catalysis and selectivity, pliability of the His-loop and the position of the propeller blades are adjusted	Pyrococcus horikoshii

Synonyms

Synonyms	Comment	Organism
PhAAP	-	Pyrococcus horikoshii

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Release 2023.1 (January 2023)