ArticleJournal of molecular biology2012
The role of the β5-α11 loop in the active-site dynamics of acylated penicillin-binding protein A from Mycobacterium tuberculosis.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Molecular insights into ochratoxin A biodegradation.Biologia futura · 2025Review
- Article
- A conserved zinc-binding site inProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Recognition of the β-lactam carboxylate triggers acylation ofThe Journal of biological chemistry · 2019Article
- The structures of penicillin-binding protein 4 (PBP4) and PBP5 fromThe Journal of biological chemistry · 2018Article
- Crystal Structures of Penicillin-Binding Protein D2 from Listeria monocytogenes and Structural Basis for Antibiotic Specificity.Antimicrobial agents and chemotherapy · 2018Article
- Review
- Optimization of a β-Lactam Scaffold for Antibacterial Activity via the Inhibition of Bacterial Type I Signal Peptidase.ACS medicinal chemistry letters · 2018Article
- The Growing Genetic and Functional Diversity of Extended Spectrum Beta-Lactamases.BioMed research international · 2018Review
- Resistance to antibiotics targeted to the bacterial cell wall.Protein science : a publication of the Protein Society · 2014Review
- Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis.PloS one · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Penicillin-binding protein A (PBPA) is a class B penicillin-binding protein that is important for cell division in Mycobacterium tuberculosis. We have determined a second crystal structure of PBPA in apo form and compared it with an earlier structure of apoenzyme. Significant structural differences in the active site region are apparent, including increased ordering of a β-hairpin loop and a shift of the SxN active site motif such that it now occupies a position that appears catalytically competent. Using two assays, including one that uses the intrinsic fluorescence of a tryptophan residue, we have also measured the second-order acylation rate constants for the antibiotics imipenem, penicillin G, and ceftriaxone. Of these, imipenem, which has demonstrable anti-tubercular activity, shows the highest acylation efficiency. Crystal structures of PBPA in complex with the same antibiotics were also determined, and all show conformational differences in the β5-α11 loop near the active site, but these differ for each β-lactam and also for each of the two molecules in the crystallographic asymmetric unit. Overall, these data reveal the β5-α11 loop of PBPA as a flexible region that appears important for acylation and provide further evidence that penicillin-binding proteins in apo form can occupy different conformational states.
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Registered trials
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.