ArticleProceedings of the National Academy of Sciences of the United States of America2005
Active site restructuring regulates ligand recognition in class A penicillin-binding proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 103 citations in OpenAlex.
- A novel penicillin-binding protein inhibitor with unprecedented intracellular activity eradicates multiple pathogenic bacteria.PLoS pathogens · 2026Article
- Structural and Dynamics Analyses of β-Lactam Inhibition ofACS chemical biology · 2026Article
- Structure-Activity Relationship and Crystallographic Study of New Monobactams.Journal of medicinal chemistry · 2026Article
- Target Fidelity and Failure: Structure-Activity Relationship of High-Molecular-Mass Penicillin-Binding Proteins (HMM-PBPs) in RefractoryAntibiotics (Basel, Switzerland) · 2026Article
- Antibiotic resistance in Helicobacter pylori: a genetic and physiological perspective.Gut pathogens · 2025Review
- Alpha and Omega Classification of β-Lactamase/Transpeptidase-like Superfamily Proteins Based on the Comparison of Their Structural Catalytic Cores.Molecules (Basel, Switzerland) · 2025Article
- Metabolic profiling and antimicrobial activity ofFrontiers in pharmacology · 2025Article
- Boronic acid inhibitors of penicillin-binding protein 1b: serine and lysine labelling agents.Journal of enzyme inhibition and medicinal chemistry · 2024Article
- Plant-Derived Antimicrobials and Their Crucial Role in Combating Antimicrobial Resistance.Antibiotics (Basel, Switzerland) · 2024Review
- Combined Structural Analysis and Molecular Dynamics Reveal Penicillin-Binding Protein Inhibition Mode with β-Lactones.ACS chemical biology · 2022Article
- Synergistic Role of Plant Extracts and Essential Oils against Multidrug Resistance and Gram-Negative Bacterial Strains Producing Extended-Spectrum β-Lactamases.Antibiotics (Basel, Switzerland) · 2022Review
- Metabolite fingerprinting of phytoconstituents from Fritillaria cirrhosa D. Don and molecular docking analysis of bioactive peonidin with microbial drug target proteins.Scientific reports · 2022Article
- Comparative Genomic Analysis of Streptococcus pneumoniae Strains: Penicillin Non-susceptible Multi-drug-Resistant Serotype 19A Isolates.Current microbiology · 2022Article
- β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.Cold Spring Harbor perspectives in medicine · 2016Review
- Computational analysis of candidate prion-like proteins in bacteria and their role.Frontiers in microbiology · 2015Article
- 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
- Crystal structures of bifunctional penicillin-binding protein 4 from Listeria monocytogenes.Antimicrobial agents and chemotherapy · 2013Article
- Utilization of protein intrinsic disorder knowledge in structural proteomics.Biochimica et biophysica acta · 2013Article
- Structural insights into the anti-methicillin-resistant Staphylococcus aureus (MRSA) activity of ceftobiprole.The Journal of biological chemistry · 2012Article
- The role of the β5-α11 loop in the active-site dynamics of acylated penicillin-binding protein A from Mycobacterium tuberculosis.Journal of molecular biology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial cell division is a complex, multimolecular process that requires biosynthesis of new peptidoglycan by penicillin-binding proteins (PBPs) during cell wall elongation and septum formation steps. Streptococcus pneumoniae has three bifunctional (class A) PBPs that catalyze both polymerization of glycan chains (glycosyltransfer) and cross-linking of pentapeptidic bridges (transpeptidation) during the peptidoglycan biosynthetic process. In addition to playing important roles in cell division, PBPs are also the targets for beta-lactam antibiotics and thus play key roles in drug-resistance mechanisms. The crystal structure of a soluble form of pneumococcal PBP1b (PBP1b*) has been solved to 1.9 A, thus providing previously undescribed structural information regarding a class A PBP from any organism. PBP1b* is a three-domain molecule harboring a short peptide from the glycosyltransferase domain bound to an interdomain linker region, the transpeptidase domain, and a C-terminal region. The structure of PBP1b* complexed with beta-lactam antibiotics reveals that ligand recognition requires a conformational modification involving conserved elements within the cleft. The open and closed structures of PBP1b* suggest how class A PBPs may become activated as novel peptidoglycan synthesis becomes necessary during the cell division process. In addition, this structure provides an initial framework for the understanding of the role of class A PBPs in the development of antibiotic resistance.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.