ArticleNature communications2021
Structural basis of the membrane intramolecular transacylase reaction responsible for lyso-form lipoprotein synthesis.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Reconstitution of the LnsAB lipoprotein N-acylation system complex from Staphylococcus aureus and characterization of substrate preference.The Journal of biological chemistry · 2026Article
- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
- Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification and Characterization of the LipoproteinbioRxiv : the preprint server for biology · 2024Article
- Structure snapshots reveal the mechanism of a bacterial membrane lipoproteinScience advances · 2023Article
- The Extracellular Electron Transport Pathway Reduces Copper for Sensing by the CopRS Two-Component System under Anaerobic Conditions in Listeria monocytogenes.Journal of bacteriology · 2023Article
- A Copper-Responsive Two-Component System Governs Lipoprotein Remodeling in Listeria monocytogenes.Journal of bacteriology · 2023Article
- Effects of extracellular vesicles derived from oral bacteria on osteoclast differentiation and activation.Scientific reports · 2022Article
- Bacterial Lipoprotein Posttranslational Modifications. New Insights and Opportunities for Antibiotic and Vaccine Development.Frontiers in microbiology · 2021Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoproteins serve diverse functions in the bacterial cell and some are essential for survival. Some lipoproteins are adjuvants eliciting responses from the innate immune system of the host. The growing list of membrane enzymes responsible for lipoprotein synthesis includes the recently discovered lipoprotein intramolecular transacylase, Lit. Lit creates a lipoprotein that is less immunogenic, possibly enabling the bacteria to gain a foothold in the host by stealth. Here, we report the crystal structure of the Lit enzyme from Bacillus cereus and describe its mechanism of action. Lit consists of four transmembrane helices with an extracellular cap. Conserved residues map to the cap-membrane interface. They include two catalytic histidines that function to effect unimolecular transacylation. The reaction involves acyl transfer from the sn-2 position of the glyceryl moiety to the amino group on the N-terminal cysteine of the substrate via an 8-membered ring intermediate. Transacylation takes place in a confined aromatic residue-rich environment that likely evolved to bring distant moieties on the substrate into proximity and proper orientation for catalysis.
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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.