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 | Comment | Organism |
---|---|---|
S187A | a proteolytically inactive hexameric enzyme mutant | Escherichia coli K-12 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Escherichia coli K-12 | - |
- |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli K-12 | P39099 | - |
- |
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 | 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 | Comment | Organism |
---|---|---|
DegQ | - |
Escherichia coli K-12 |
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 |