Literature summary for 3.4.21.105 extracted from

Uritsky, N.; Shokhen, M.; Albeck, A.
The catalytic machinery of rhomboid proteases: Combined MD and QM simulations (2012), J. Chem. Theory Comput., 8, 4663-4671.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulation. In both membrane and lipid-solubilized environments the S201/H254 and S201/H150 interatomic distances of GlpG are most sensitive to variations of the protonation state of the active site residues. The catalytic diad of the lipid-solubilized enzyme exists as an H254(+)-S201(-) ion pair at the Michaelis complex stage, with Ser201 ready for nucleophilic attack on the substrate. Therefore, deprotonation of S201 does not contribute to the activation barrier of covalent tetrahedral complex formation. Both catalytic residues, H254 and S201, are neutral in the Michaelis complex of GlpG in the membrane. Therefore, S201 deprotonation by H254 general base catalysis should contribute to the activation barrier of the covalent tetrahedral complex formation	Escherichia coli

Crystallization (Comment)

Organism

molecular dynamics simulation. In both membrane and lipid-solubilized environments the S201/H254 and S201/H150 interatomic distances of GlpG are most sensitive to variations of the protonation state of the active site residues. The catalytic diad of the lipid-solubilized enzyme exists as an H254(+)-S201(-) ion pair at the Michaelis complex stage, with Ser201 ready for nucleophilic attack on the substrate. Therefore, deprotonation of S201 does not contribute to the activation barrier of covalent tetrahedral complex formation. Both catalytic residues, H254 and S201, are neutral in the Michaelis complex of GlpG in the membrane. Therefore, S201 deprotonation by H254 general base catalysis should contribute to the activation barrier of the covalent tetrahedral complex formation

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09391	-	-

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Release 2023.1 (January 2023)