Crystallization (Comment) | Organism |
---|---|
a theoretical model of the three-dimensional structure of the LA loop as per the resting state of enzyme HtrA. hydrophobic interactions connect the LA loops of the hexamer and polar contacts between the LA', i.e. the LA loop on an opposite subunit, and L1 loops on opposite subunits. Disturbance of these interactions causes the stimulation of HtrA proteolytic activity. LA loops contribute to the preservation of the integrity of the HtrA oligomer and to the stability of the monomer | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D52A | mutation within LA loop. Mutation has no impact on the proteolytic activity of HtrA | Escherichia coli |
D53A | mutation within LA loop. Mutation has no impact on the proteolytic activity of HtrA | Escherichia coli |
F46Y | mutation within LA loop. Mutant displays increased activity with substrate beta-casein | Escherichia coli |
F49Y/F50Y | mutation within LA loop. Mutant displays increased activity with substrate beta-casein | Escherichia coli |
F50W/S210A | catalytically inactive mutant | Escherichia coli |
F56S | mutation within LA loop. Mutation has no impact on the proteolytic activity of HtrA | Escherichia coli |
F63Y | mutation within LA loop. Mutant displays increased activity with substrate beta-casein | Escherichia coli |
F68Y | mutation within LA loop. Mutant displays increased activity with substrate beta-casein | Escherichia coli |
P43G | mutation within LA loop. At 20 °C the activities of are similar to wild-type, whereas at higher temperatures of 35 or 45 °C the mutant shows a higher activity | Escherichia coli |
Q47L | mutation within LA loop. Mutant displays increased activity with substrate beta-casein | Escherichia coli |
Q64A | mutation within LA loop. Mutation has no impact on the proteolytic activity of HtrA | Escherichia coli |
Q64I | mutation within LA loop. Mutation has no impact on the proteolytic activity of HtrA | Escherichia coli |
Q70A | mutation within LA loop. Mutant displays increased activity with substrate beta-casein | Escherichia coli |
R44A | mutation within LA loop. Mutation leads to dramatic autocleavage of the protein, occurring both within cells and during their preparation | Escherichia coli |
R44A/F50W/S210A | catalytically inactive mutant | Escherichia coli |
S54A | mutation within LA loop. Mutation has no impact on the proteolytic activity of HtrA | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Escherichia coli | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0C0V0 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-casein + H2O | - |
Escherichia coli | ? | - |
? |