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Literature summary for 3.4.16.4 extracted from

  • Hargis, J.; Vankayala, S.; White, J.; Woodcock, H.
    Identification and characterization of noncovalent interactions that drive binding and specificity in DD-peptidases and beta-lactamases (2014), J. Chem. Theory Comput., 10, 855-864.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
characterization of the noncovalent interactions based on cocrystallized structures of benzylpenicillin and perfect penicillin covalently bound to DD-peptidase by computational methods. Benzylpenicillin’s phenyl group forms an extended pi?pi network with Phe120 and Trp233 that contributes significantly to its efficacy in DD-peptidase. This aromatic stabilization is conserved in beta-lactamases. Interactions between the protein and the peptidomimetic tail region, particularly carboxylate 2 and the terminal N4H3+ unit, form unique hydrogen bonding and strong electrostatic interactions. Between Asp217 and the N4H3+ there is a water mediated salt bridge Streptomyces sp.

Organism

Organism UniProt Comment Textmining
Streptomyces sp. P15555
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