ArticleStructure (London, England : 1993)2021
Structure-based modeling and dynamics of MurM, a Streptococcus pneumoniae penicillin resistance determinant present at the cytoplasmic membrane.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Structural and biochemical insights into the antibiofilm activity of cationic lipoamino acid ester against methicillin-resistantRSC advances · 2026Article
- Aminoacyl-tRNA-dependent enzymes in natural product biosynthesis: structure-function insights.The Journal of antibiotics · 2026Review
- The effect of MurM and a branched cell wall structure on penicillin resistance inJournal of bacteriology · 2025Article
- Review
- Discovery of potential natural therapeutics targeting cell wall biosynthesis in multidrug-resistant Enterococcus faecalis: a computational perspective.Biology direct · 2024Article
- Cloning, Purification, and Biophysical Characterization of FemB Protein from Methicillin-Resistant Staphylococcus aureus and Inhibitors Screening.Applied biochemistry and biotechnology · 2024Article
- Integrative multi-omics deciphers the spatial characteristics of host-gut microbiota interactions in Crohn's disease.Cell reports. Medicine · 2023Article
- Subcellular localization of the enterobacterial common antigen GT-E-like glycosyltransferase, WecG.Molecular microbiology · 2022Article
- What have molecular simulations contributed to understanding of Gram-negative bacterial cell envelopes?Microbiology (Reading, England) · 2022Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Branched Lipid II, required for the formation of indirectly crosslinked peptidoglycan, is generated by MurM, a protein essential for high-level penicillin resistance in the human pathogen Streptococcus pneumoniae. We have solved the X-ray crystal structure of Staphylococcus aureus FemX, an isofunctional homolog, and have used this as a template to generate a MurM homology model. Using this model, we perform molecular docking and molecular dynamics to examine the interaction of MurM with the phospholipid bilayer and the membrane-embedded Lipid II substrate. Our model suggests that MurM is associated with the major membrane phospholipid cardiolipin, and experimental evidence confirms that the activity of MurM is enhanced by this phospholipid and inhibited by its direct precursor phosphatidylglycerol. The spatial association of pneumococcal membrane phospholipids and their impact on MurM activity may therefore be critical to the final architecture of peptidoglycan and the expression of clinically relevant penicillin resistance in this pathogen.
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