ArticlePloS one2014
Crystal structure of penicillin-binding protein 3 (PBP3) from Escherichia coli.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
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- From genomics to treatment: overcoming pan-drug-resistantFrontiers in pharmacology · 2025Article
- In Vivo Cross-Linking Sheds Light on the Salmonella Divisome in Which PBP3 and PBP3Molecular microbiology · 2024Article
- Antibacterial activities, PASS prediction and ADME analysis of phytochemicals fromIn silico pharmacology · 2024Article
- Comparative genomics hints at dispensability of multiple essential genes in two Escherichia coli L-form strains.Bioscience reports · 2023Article
- The structural integrity of the membrane-embedded bacterial division complex FtsQBL studied with molecular dynamics simulations.Computational and structural biotechnology journal · 2023Article
- Advanced transcriptomic analysis reveals the role of efflux pumps and media composition in antibiotic responses of Pseudomonas aeruginosa.Nucleic acids research · 2022Article
- A unique class of ZnNature communications · 2022Article
- Macromolecular Structure Assembly as a Novel Antibiotic Target.Antibiotics (Basel, Switzerland) · 2022Article
- The Bacterial Cell Wall: From Lipid II Flipping to Polymerization.Chemical reviews · 2022Review
- An Updated Model of the Divisome: Regulation of the Septal Peptidoglycan Synthesis Machinery by the Divisome.International journal of molecular sciences · 2022Review
- Interaction Mode of the Novel Monobactam AIC499 Targeting Penicillin Binding Protein 3 of Gram-Negative Bacteria.Biomolecules · 2021Article
- Demonstration of the utility of DOS-derived fragment libraries for rapid hit derivatisation in a multidirectional fashion.Chemical science · 2020Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, penicillin-binding protein 3 (PBP3), also known as FtsI, is a central component of the divisome, catalyzing cross-linking of the cell wall peptidoglycan during cell division. PBP3 is mainly periplasmic, with a 23 residues cytoplasmic tail and a single transmembrane helix. We have solved the crystal structure of a soluble form of PBP3 (PBP3(57-577)) at 2.5 Å revealing the two modules of high molecular weight class B PBPs, a carboxy terminal module exhibiting transpeptidase activity and an amino terminal module of unknown function. To gain additional insight, the PBP3 Val88-Ser165 subdomain (PBP3(88-165)), for which the electron density is poorly defined in the PBP3 crystal, was produced and its structure solved by SAD phasing at 2.1 Å. The structure shows a three dimensional domain swapping with a β-strand of one molecule inserted between two strands of the paired molecule, suggesting a possible role in PBP3(57-577) dimerization.
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