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Literature summary for 3.4.11.7 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 .
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Thermoplasma acidophilum O93655
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Purification (Commentary)

Purification (Comment) Organism
-
Thermoplasma acidophilum

Synonyms

Synonyms Comment Organism
tricorn interacting factor F3
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Thermoplasma acidophilum
tricorn protease-interacting factor F3
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Thermoplasma acidophilum