ArticleStructure (London, England : 1993)2014
Elongated structure of the outer-membrane activator of peptidoglycan synthesis LpoA: implications for PBP1A stimulation.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed.
- Clinical characteristics, specific resistance patterns, and molecular mechanisms of carbapenem-resistantFrontiers in cellular and infection microbiology · 2025Article
- Article
- The unique 3D arrangement of macrophage galactose lectin enablesPNAS nexus · 2023Article
- Escherichia coli has robust regulatory mechanisms against elevated peptidoglycan cleavage by lytic transglycosylases.The Journal of biological chemistry · 2023Article
- Outer membrane-anchoring enables LpoB to regulate peptidoglycan synthesis rate.Cell surface (Amsterdam, Netherlands) · 2022Article
- Article
- Early midcell localization of Escherichia coli PBP4 supports the function of peptidoglycan amidases.PLoS genetics · 2022Article
- What Is Motion? Recent Advances in the Study of Molecular Movement Patterns of the Peptidoglycan Synthesis Machines.Journal of bacteriology · 2022Review
- Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands.Cell surface (Amsterdam, Netherlands) · 2021Article
- A Dynamic Network of Proteins Facilitate Cell Envelope Biogenesis in Gram-Negative Bacteria.International journal of molecular sciences · 2021Review
- The LpoA activator is required to stimulate the peptidoglycan polymerase activity of its cognate cell wall synthase PBP1a.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins.eLife · 2021Article
- Peptidoglycan: Structure, Synthesis, and Regulation.EcoSal Plus · 2021Article
- Review
- Regulation of peptidoglycan synthesis and remodelling.Nature reviews. Microbiology · 2020Review
- Article
- Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa.Structure (London, England : 1993) · 2020Article
- Characterizing Membrane Association and Periplasmic Transfer of Bacterial Lipoproteins through Molecular Dynamics Simulations.Structure (London, England : 1993) · 2020Article
- Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi-enzyme complexes in Escherichia coli.The EMBO journal · 2020Article
- Class-A penicillin binding proteins do not contribute to cell shape but repair cell-wall defects.eLife · 2020Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
The bacterial cell envelope contains the stress-bearing peptidoglycan layer, which is enlarged during cell growth and division by membrane-anchored synthases guided by cytoskeletal elements. In Escherichia coli, the major peptidoglycan synthase PBP1A requires stimulation by the outer-membrane-anchored lipoprotein LpoA. Whereas the C-terminal domain of LpoA interacts with PBP1A to stimulate its peptide crosslinking activity, little is known about the role of the N-terminal domain. Herein we report its NMR structure, which adopts an all-α-helical fold comprising a series of helix-turn-helix tetratricopeptide-repeat (TPR)-like motifs. NMR spectroscopy of full-length LpoA revealed two extended flexible regions in the C-terminal domain and limited, if any, flexibility between the N- and C-terminal domains. Analytical ultracentrifugation and small-angle X-ray scattering results are consistent with LpoA adopting an elongated shape, with dimensions sufficient to span from the outer membrane through the periplasm to interact with the peptidoglycan synthase PBP1A.
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Registered trials
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