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Literature summary for 3.4.21.105 extracted from

  • Vinothkumar, K.R.; Pierrat, O.A.; Large, J.M.; Freeman, M.
    Structure of rhomboid protease in complex with beta-lactam inhibitors defines the S2 cavity (2013), Structure, 21, 1051-1058.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure in complex with beta-lactam inhibitors phenyl 2-oxo-4-phenylazetidine-1-carboxylate, 2-methylpropyl 2-oxo-4-phenylazetidine-1-carboxylate, and cyclopentyl 2-oxo-4-phenylazetidine-1-carboxylate, to 2.2 to 2.4 A resolution Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-methylpropyl 2-oxo-4-phenylazetidine-1-carboxylate beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site Escherichia coli
cyclopentyl 2-oxo-4-phenylazetidine-1-carboxylate beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site Escherichia coli
phenyl 2-oxo-4-phenylazetidine-1-carboxylate beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P09391
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