ArticleNature2015
Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 98 citations in OpenAlex.
- Architecture of an asymmetric short chain/long chain hybrid acyl‑CoA carboxylase from Mycobacterium smegmatis.Communications biology · 2026Article
- Oligomeric assemblies of plant biotin carboxylase revealed by cryo-EM and cross-linking.The Biochemical journal · 2026Article
- Insights Into circRNA-Mediated Lipid Metabolism in Cancer Progression.Journal of cellular and molecular medicine · 2026Review
- Assessing Acetyl-Coenzyme A Carboxylase Activity and Inhibition inAnalytical chemistry · 2025Article
- A new class of natural anthelmintics targeting lipid metabolism.Nature communications · 2025Article
- Plant acetyl-CoA carboxylase: The homomeric form and the heteromeric form.BBA advances · 2025Article
- Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase.Nature structural & molecular biology · 2025Article
- Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase.Science advances · 2024Article
- ActivebioRxiv : the preprint server for biology · 2024Article
- Article
- Sample optimizations to enable the structure determination of biotin-dependent carboxylases.Methods in enzymology · 2024Article
- Allosteric Site at the Biotin Carboxylase Dimer Interface Mediates Activation and Inhibition inBiochemistry · 2023Article
- Article
- Metabolic Engineering and Synthetic Biology Approaches for the Heterologous Production of Aromatic Polyketides.International journal of molecular sciences · 2023Review
- Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase.Structure (London, England : 1993) · 2023Article
- The opportunistic pathogen Pseudomonas aeruginosa exploits bacterial biotin synthesis pathway to benefit its infectivity.PLoS pathogens · 2023Article
- Heterobivalent Inhibitors of Acetyl-CoA Carboxylase: Drug Target Residence Time and Time-Dependent Antibacterial Activity.Journal of medicinal chemistry · 2022Article
- CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.Nature communications · 2022Article
- AMPK signaling and its targeting in cancer progression and treatment.Seminars in cancer biology · 2022Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Acetyl-CoA carboxylase (ACC) has crucial roles in fatty acid metabolism and is an attractive target for drug discovery against diabetes, cancer and other diseases. Saccharomyces cerevisiae ACC (ScACC) is crucial for the production of very-long-chain fatty acids and the maintenance of the nuclear envelope. ACC contains biotin carboxylase (BC) and carboxyltransferase (CT) activities, and its biotin is linked covalently to the biotin carboxyl carrier protein (BCCP). Most eukaryotic ACCs are 250-kilodalton (kDa), multi-domain enzymes and function as homodimers and higher oligomers. They contain a unique, 80-kDa central region that shares no homology with other proteins. Although the structures of the BC, CT and BCCP domains and other biotin-dependent carboxylase holoenzymes are known, there is currently no structural information on the ACC holoenzyme. Here we report the crystal structure of the full-length, 500-kDa holoenzyme dimer of ScACC. The structure is remarkably different from that of the other biotin-dependent carboxylases. The central region contains five domains and is important for positioning the BC and CT domains for catalysis. The structure unexpectedly reveals a dimer of the BC domain and extensive conformational differences compared to the structure of the BC domain alone, which is a monomer. These structural changes reveal why the BC domain alone is catalytically inactive and define the molecular mechanism for the inhibition of eukaryotic ACC by the natural product soraphen A and by phosphorylation of a Ser residue just before the BC domain core in mammalian ACC. The BC and CT active sites are separated by 80 Å, and the entire BCCP domain must translocate during catalysis.
Indexed as
Identifiers
What OpenQuestion holds
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.