ArticleStructure (London, England : 1993)2013
The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Oligomeric assemblies of plant biotin carboxylase revealed by cryo-EM and cross-linking.The Biochemical journal · 2026Article
- Article
- Plant acetyl-CoA carboxylase: The homomeric form and the heteromeric form.BBA advances · 2025Article
- Bioinformatics study of biotin carboxylase B-subdomain isolated fromBiotechnologia · 2025Article
- ActivebioRxiv : the preprint server for biology · 2024Article
- Article
- Purification of heteromeric acetyl-CoA carboxylases from Escherichia coli for structure solution.Methods in enzymology · 2024Article
- Heterobivalent Inhibitors of Acetyl-CoA Carboxylase: Drug Target Residence Time and Time-Dependent Antibacterial Activity.Journal of medicinal chemistry · 2022Article
- Metabolic and Structural Insights into Hydrogen Sulfide Mis-Regulation inAntioxidants (Basel, Switzerland) · 2022Article
- Acetyl-CoA Carboxylases and Diseases.Frontiers in oncology · 2022Review
- The Classical, Yet Controversial, First Enzyme of Lipid Synthesis: Escherichia coli Acetyl-CoA Carboxylase.Microbiology and molecular biology reviews : MMBR · 2021Review
- Increasing the Ascomycin Yield by Relieving the Inhibition of Acetyl/Propionyl-CoA Carboxylase by the Signal Transduction Protein GlnB.Frontiers in microbiology · 2021Article
- The BADC and BCCP subunits of chloroplast acetyl-CoA carboxylase sense the pH changes of the light-dark cycle.The Journal of biological chemistry · 2020Article
- Non-Catalytic Subunits Facilitate Quaternary Organization of Plastidic Acetyl-CoA Carboxylase.Plant physiology · 2020Article
- Crystal structure of the essential biotin-dependent carboxylase AccA3 fromFEBS open bio · 2017Article
- A Family of Negative Regulators Targets the Committed Step of de Novo Fatty Acid Biosynthesis.The Plant cell · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Acetyl-coenzyme A (acetyl-CoA) carboxylase is a biotin-dependent, multifunctional enzyme that catalyzes the regulated step in fatty acid synthesis. The Escherichia coli enzyme is composed of a homodimeric biotin carboxylase (BC), biotinylated biotin carboxyl carrier protein (BCCP), and an α2β2 heterotetrameric carboxyltransferase. This enzyme complex catalyzes two half-reactions to form malonyl-coenzyme A. BC and BCCP participate in the first half-reaction, whereas carboxyltransferase and BCCP are involved in the second. Three-dimensional structures have been reported for the individual subunits; however, the structural basis for how BCCP reacts with the carboxylase or transferase is unknown. Therefore, we report here the crystal structure of E. coli BCCP complexed with BC to a resolution of 2.49 Å. The protein-protein complex shows a unique quaternary structure and two distinct interfaces for each BCCP monomer. These BCCP binding sites are unique compared to phylogenetically related biotin-dependent carboxylases and therefore provide novel targets for developing antibiotics against bacterial acetyl-CoA carboxylase.
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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.