ArticleNature communications2018
Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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Who cites it
23 citing papers in PubMed, 56 citations in OpenAlex.
- Spider Venom Peptides as Potential Allosteric Inhibitors of Undecaprenyl Diphosphatase (UppP) fromToxins · 2026Article
- Pardon the interruption: how Und-P sequestration has reshaped our understanding of the bacterial cell envelope.Journal of bacteriology · 2026Review
- Ligand-based discovery of novel N-arylpyrrole derivatives as broad-spectrum antimicrobial agents with antibiofilm and anti-virulence activity.Journal of enzyme inhibition and medicinal chemistry · 2025Article
- Lipopeptide antibiotics disrupt interactions of undecaprenyl phosphate with UptA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Providing insight into the mechanism of action of cationic lipidated oligomers using metabolomics.mSystems · 2024Article
- Real-Time Biosynthetic Reaction Monitoring Informs the Mechanism of Action of Antibiotics.Journal of the American Chemical Society · 2024Article
- Investigation into the Mechanism of Action of the Tuberculosis Drug Candidate SQ109 and Its Metabolites and Analogues in Mycobacteria.Journal of medicinal chemistry · 2023Article
- Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022Review
- The Bacterial Cell Wall: From Lipid II Flipping to Polymerization.Chemical reviews · 2022Review
- Mechanistic insights into the CChemical science · 2022Article
- Regulation of ER-derived membrane dynamics by the DedA domain-containing proteins VMP1 and TMEM41B.EMBO reports · 2022Review
- Towards discovery of inhibitors of the undecaprenyl-pyrophosphate phosphatase BacA by virtual high-throughput screening.Computational and structural biotechnology journal · 2022Article
- Mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- β-Lactams against the Fortress of the Gram-PositiveChemical reviews · 2021Review
- Structure, catalysis, and inhibition mechanism of prenyltransferase.IUBMB life · 2021Review
- AFrontiers in microbiology · 2020Article
- Investigation of the conserved reentrant membrane helix in the monotopic phosphoglycosyl transferase superfamily supports key molecular interactions with polyprenol phosphate substrates.Archives of biochemistry and biophysics · 2019Article
- Pyruvate Substitutions on Glycoconjugates.International journal of molecular sciences · 2019Review
- Cell wall peptidoglycan in Mycobacterium tuberculosis: An Achilles' heel for the TB-causing pathogen.FEMS microbiology reviews · 2019Review
- HupA, the main undecaprenyl pyrophosphate and phosphatidylglycerol phosphate phosphatase in Helicobacter pylori is essential for colonization of the stomach.PLoS pathogens · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Undecaprenyl pyrophosphate phosphatase (UppP) is an integral membrane protein that recycles the lipid carrier essential to the ongoing biosynthesis of the bacterial cell wall. Individual building blocks of peptidoglycan are assembled in the cytoplasm on undecaprenyl phosphate (C55-P) before being flipped to the periplasmic face, where they are polymerized and transferred to the existing cell wall sacculus, resulting in the side product undecaprenyl pyrophosphate (C55-PP). Interruption of UppP's regeneration of C55-P from C55-PP leads to the buildup of cell wall intermediates and cell lysis. We present the crystal structure of UppP from Escherichia coli at 2.0 Å resolution, which reveals the mechanistic basis for intramembranal phosphatase action and substrate specificity using an inverted topology repeat. In addition, the observation of key structural motifs common to a variety of cross membrane transporters hints at a potential flippase function in the specific relocalization of the C55-P product back to the cytosolic space.
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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.