Literature summary extracted from

Kyrieleis, O.; Goettig, P.; Kiefersauer, R.; Huber, R.; Brandstetter, H.
Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations (2005), J. Mol. Biol., 349, 787-800 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.4.11.7	expression in Escherichia coli BL21(DE3)	Thermoplasma acidophilum

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.4.11.7	hexagonal crystals of F3 are grown from 0.1 M Tris-HCl (pH 8.5), 18% (w/w) PEG 2000 and 0.2 M Li2SO4 at 18°C using the sitting-drop, vapor-diffusion technique. Crystal structure of the tricorn interacting factor F3 in free form and in three different conformations, depending on the crystal form in which they are crystallized, give insights into the molecular dynamics of F3 relating to substrate binding and mechanistic aspects of substrate processing. The structure adumbrates how F3 might assemble with the tricorn protease and how the substrate transfer from the tricorn protease to F3 might proceed	Thermoplasma acidophilum

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.11.7	Thermoplasma acidophilum	O93655	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.4.11.7	-	Thermoplasma acidophilum

Synonyms

EC Number	Synonyms	Comment	Organism
3.4.11.7	tricorn interacting factor F3	-	Thermoplasma acidophilum
3.4.11.7	tricorn protease-interacting factor F3	-	Thermoplasma acidophilum

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Release 2023.1 (January 2023)