ArticleJournal of the American Chemical Society2011
A computational evaluation of the mechanism of penicillin-binding protein-catalyzed cross-linking of the bacterial cell wall.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Structural and Dynamics Analyses of β-Lactam Inhibition ofACS chemical biology · 2026Article
- Conformational analysis of different tautomers of some antibiotics.Journal of molecular modeling · 2026Article
- Airway microbiota and immunity associated with chronic obstructive pulmonary disease severity.Journal of translational medicine · 2025Article
- Boronic acid inhibitors of penicillin-binding protein 1b: serine and lysine labelling agents.Journal of enzyme inhibition and medicinal chemistry · 2024Article
- Unconventional Antibacterials and Adjuvants.Accounts of chemical research · 2021Article
- Integrative structural biology of the penicillin-binding protein-1 fromComputational and structural biotechnology journal · 2021Article
- Conformational Dynamics in Penicillin-Binding Protein 2a of Methicillin-Resistant Staphylococcus aureus, Allosteric Communication Network and Enablement of Catalysis.Journal of the American Chemical Society · 2017Article
- Detection of lipid-linked peptidoglycan precursors by exploiting an unexpected transpeptidase reaction.Journal of the American Chemical Society · 2014Article
- Reconstitution of peptidoglycan cross-linking leads to improved fluorescent probes of cell wall synthesis.Journal of the American Chemical Society · 2014Article
- Review
- Protonation states of active-site lysines of penicillin-binding protein 6 from Escherichia coli and the mechanistic implications.Proteins · 2014Article
- Lipoprotein activators stimulate Escherichia coli penicillin-binding proteins by different mechanisms.Journal of the American Chemical Society · 2014Article
- How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological function.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Reaction products and the X-ray structure of AmpDh2, a virulence determinant of Pseudomonas aeruginosa.Journal of the American Chemical Society · 2013Article
- Bacterial cell-wall recycling.Annals of the New York Academy of Sciences · 2013Review
- Metallo-β-lactamase structure and function.Annals of the New York Academy of Sciences · 2013Review
- Transpeptidase-mediated incorporation of D-amino acids into bacterial peptidoglycan.Journal of the American Chemical Society · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Penicillin-binding protein 1b (PBP 1b) of the gram-positive bacterium Streptococcus pneumoniae catalyzes the cross-linking of adjacent peptidoglycan strands, as a critical event in the biosynthesis of its cell wall. This enzyme is representative of the biosynthetic PBP structures of the β-lactam-recognizing enzyme superfamily and is the target of the β-lactam antibiotics. In the cross-linking reaction, the amide between the -D-Ala-D-Ala dipeptide at the terminus of a peptide stem acts as an acyl donor toward the ε-amino group of a lysine found on an adjacent stem. The mechanism of this transpeptidation was evaluated using explicit-solvent molecular dynamics simulations and ONIOM quantum mechanics/molecular mechanics calculations. Sequential acyl transfer occurs to, and then from, the active site serine. The resulting cross-link is predicted to have a cis-amide configuration. The ensuing and energetically favorable cis- to trans-amide isomerization, within the active site, may represent the key event driving product release to complete enzymatic turnover.
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Registered trials
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