ArticleStructure (London, England : 1993)2018
Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
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- FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron.Molecular microbiology · 2023Article
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- Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022Review
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- The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.Extremophiles : life under extreme conditions · 2022Review
- Advances in the Structural Biology, Mechanism, and Physiology of Cyclopropane Fatty Acid Modifications of Bacterial Membranes.Microbiology and molecular biology reviews : MMBR · 2022Review
- Multi-Omic Analysis to Characterize Metabolic Adaptation of theMetabolites · 2022Article
- Diversity of the reaction mechanisms of SAM-dependent enzymes.Acta pharmaceutica Sinica. B · 2021Review
- Native-like membrane models of E. coli polar lipid extract shed light on the importance of lipid composition complexity.BMC biology · 2021Article
- Production of 10-methyl branched fatty acids in yeast.Biotechnology for biofuels · 2021Article
- Comparative Review of the Responses ofGenes · 2020Review
- Salmonella enterica Serovar Typhimurium Uses PbgA/YejM To Regulate Lipopolysaccharide Assembly during Bacteremia.Infection and immunity · 2019Article
- Bacterial Cyclopropane Fatty Acid Synthase mRNA Is Targeted by Activating and Repressing Small RNAs.Journal of bacteriology · 2019Article
- Gut microbiota-derived fatty acid and sterol metabolites: biotransformation and immunomodulatory functions.Gut microbesReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cell membranes must adapt to different environments. In Gram-negative bacteria, the inner membrane can be remodeled directly by modification of lipids embedded in the bilayer. For example, when Escherichia coli enters stationary phase, cyclopropane fatty acid (CFA) synthase converts most double bonds in unsaturated inner-membrane lipids into cyclopropyl groups. Here we report the crystal structure of E. coli CFA synthase. The enzyme is a dimer in the crystal and in solution, with each subunit containing a smaller N-domain that associates tightly with a larger catalytic C-domain, even following cleavage of the inter-domain linker or co-expression of each individual domain. Efficient catalysis requires dimerization and proper linkage of the two domains. These findings support an avidity-based model in which one subunit of the dimer stabilizes membrane binding, while the other subunit carries out 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.