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Literature summary for 3.4.21.107 extracted from

  • Malet, H.; Canellas, F.; Sawa, J.; Yan, J.; Thalassinos, K.; Ehrmann, M.; Clausen, T.; Saibil, H.R.
    Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ (2012), Nat. Struct. Mol. Biol., 19, 152-157.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.107

Crystallization (Commentary)

Crystallization (Comment) Organism
structure determination and analysis of the 24meric enzyme with complexed substrate beta-casein, cryo-electron microscopy images and three-dimensional structures, overview Escherichia coli K-12

Protein Variants

Protein Variants Comment Organism
S187A a proteolytically inactive hexameric enzyme mutant Escherichia coli K-12

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Escherichia coli K-12
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44835
-
 12 * 44835, mass spectrometry Escherichia coli K-12
44835
-
 24 * 44835, mass spectrometry Escherichia coli K-12
44835
-
 6 * 44835, mass spectrometry Escherichia coli K-12
44840
-
 enzyme monomer, mass spectrometry Escherichia coli K-12
270100
-
 enzyme dodecamer, mass spectrometry Escherichia coli K-12
553100
-
 enzyme tetracosamer, mass spectrometry Escherichia coli K-12

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli K-12 the enzyme shows chaperone-like activity with substrate lysozyme, and protease activity. The PDZ domains are needed for DegQ chaperone activity. Up to six lysozyme substrates bind inside the DegQ dodecamer cage, binding of a well-ordered lysozyme to four DegQ protomers, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12 P39099
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O
-
 Escherichia coli K-12 ?
-
 ?
additional information the enzyme shows chaperone-like activity with substrate lysozyme, and protease activity. The PDZ domains are needed for DegQ chaperone activity. Up to six lysozyme substrates bind inside the DegQ dodecamer cage, binding of a well-ordered lysozyme to four DegQ protomers, overview Escherichia coli K-12 ?
-
 ?

Subunits

Subunits Comment Organism
dodecamer 12 * 44835, mass spectrometry Escherichia coli K-12
hexamer 6 * 44835, mass spectrometry Escherichia coli K-12
More DegQ changes its oligomeric state from hexamers to either 12 or 24mers depending on the concentration of unfolded substrate, DegQ forms 12mers in the absence of substrate at acidic pH, enzyme structure analysis of the 12 and 24mer states in complex with model substrates, overview. The polypeptides are probably cooperatively bound by PDZ1 and protease domains Escherichia coli K-12
tetracosamer 24 * 44835, mass spectrometry Escherichia coli K-12

Synonyms

Synonyms Comment Organism
DegQ
-
 Escherichia coli K-12

General Information

General Information Comment Organism
evolution the enzyme belongs to the HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. HtrA proteins are composed of a chymotrypsin-like protease domain and one (DegS, HTRA1, HTRA2) or two PDZ domains (DegP, DegQ) Escherichia coli K-12
additional information enzyme structure analysis of the 12 and 24mer states in complex with model substrates, overview. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity Escherichia coli K-12