Literature summary for 3.4.21.107 extracted from

Figaj, D.; Gieldon, A.; Polit, A.; Sobiecka-Szkatula, A.; Koper, T.; Denkiewicz, M.; Banecki, B.; Lesner, A.; Ciarkowski, J.; Lipinska, B.; Skorko-Glonek, J.
The LA loop as an important regulatory element of the HtrA (DegP) protease from Escherichia coli: structural and functional studies (2014), J. Biol. Chem., 289, 15880-15893.

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Crystallization (Commentary)

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

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

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

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0C0V0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-casein + H2O	-	Escherichia coli	?	-	?