EC Number |
---|
2.3.2.6 | 1.6 A resolution crystal structure |
2.3.2.6 | crystal structures of the Escherichia coli LF-transferase complex with phenyalanyl adenosine (rA-Phe), with or without a short peptide bearing an N-terminal Arg residue. In the presence of both the donor and acceptor substrates, the peptide formation proceedes within the crystals, and the product peptide bearing Phe at the N terminus is retained on the LF-transferase |
2.3.2.6 | enzyme adopts a monomeric structure consisting of two domains that form a bilobate molecule. The n-terminal domain forms a small lobe with an unusual fold. The large C-terminal domain has a highly conserved fold. Comparison with bacterial peptidoglycan synthase FemX |
2.3.2.6 | in complex with minimal substrate phenylalanyl adenosine inhibitor puromycin |
2.3.2.6 | in complex with puromycin. The p-methoxybenzyl group of puromycin is accomodated in a highly hydrophobic pocket. Model of complex with tRNA and a substrate bearing an N-terminal Arg or Lys |