Literature summary for 3.4.21.105 extracted from

Gaffney, K.A.; Hong, H.
The rhomboid protease GlpG has weak interaction energies in its active site hydrogen bond network (2019), J. Gen. Physiol., 151, 282-291 .

Search for more literature for 3.4.21.105

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of interaction energies among the active site residues His254, Ser201, and Asn154, which form a hydrogen bonding network. In mild detergent, the active site residues are weakly coupled with interaction energies of ?1.4 kcal/mol between His254 and Ser201 and ?0.2 kcal/mol between Ser201 and Asn154. These residues are important for function and also for the folding cooperativity of GlpG. The weak interaction between Ser and His in the catalytic dyad may partly explain the unusually slow proteolysis by GlpG	Escherichia coli

Crystallization (Comment)

Organism

analysis of interaction energies among the active site residues His254, Ser201, and Asn154, which form a hydrogen bonding network. In mild detergent, the active site residues are weakly coupled with interaction energies of ?1.4 kcal/mol between His254 and Ser201 and ?0.2 kcal/mol between Ser201 and Asn154. These residues are important for function and also for the folding cooperativity of GlpG. The weak interaction between Ser and His in the catalytic dyad may partly explain the unusually slow proteolysis by GlpG

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
H254A	complete loss of activity	Escherichia coli
N154A	complete loss of activity	Escherichia coli
N154A/H254A	mutation induces larger destabilization	Escherichia coli
N154A/S201A	mutation induces larger destabilization	Escherichia coli
S201A	complete loss of activity	Escherichia coli
S201A/H254A	double mutation on the catalytic dyad, yields a smaller decrease in the stability than individual single mutations	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09391	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)