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Literature summary for 3.4.21.B50 extracted from

  • Wrase, R.; Scott, H.; Hilgenfeld, R.; Hansen, G.
    The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies (2011), Proc. Natl. Acad. Sci. USA, 108, 10490-10495.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli KU98 cells Legionella fallonii

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method Legionella fallonii

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Legionella fallonii
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
320000 440000 gel filtration Legionella fallonii

Organism

Organism UniProt Comment Textmining
Legionella fallonii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel-affinity column chromatography, gel filtration Legionella fallonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O
-
Legionella fallonii ?
-
?
additional information DegQ does not degrade native bovine serum albumin and reductively unfolded lysozyme Legionella fallonii ?
-
?
unfolded bovine serum albumin + H2O
-
Legionella fallonii ?
-
?

Subunits

Subunits Comment Organism
dodecamer 12 * 48000-50000, dynamic light-scattering, DegQ assembles into large, cage-like dodecamers that form independently of unfolded substrate proteins. Dodecamer-formation is essential for the degradation of substrate proteins but not for the chaperone activity of DegQ Legionella fallonii

Synonyms

Synonyms Comment Organism
DegQ
-
Legionella fallonii