ArticleNature2011
An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 56 citations in OpenAlex.
- Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Substrate-enhanced filamentation of 3-methylcrotonyl-CoA carboxylase inbioRxiv : the preprint server for biology · 2025Article
- Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase.Nature structural & molecular biology · 2025Article
- The cryo-EM structure of trypanosome 3-methylcrotonyl-CoA carboxylase provides mechanistic and dynamic insights into its enzymatic function.Structure (London, England : 1993) · 2024Article
- Article
- Sample optimizations to enable the structure determination of biotin-dependent carboxylases.Methods in enzymology · 2024Article
- Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase.Structure (London, England : 1993) · 2023Article
- CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics.Journal of structural biology: X · 2023Article
- The opportunistic pathogen Pseudomonas aeruginosa exploits bacterial biotin synthesis pathway to benefit its infectivity.PLoS pathogens · 2023Article
- In silico investigation of Alsin RLD conformational dynamics and phosphoinositides binding mechanism.PloS one · 2022Article
- Biochemical and structural characterization of the BioZ enzyme engaged in bacterial biotin synthesis pathway.Nature communications · 2021Article
- MCCC2 promotes HCC development by supporting leucine oncogenic function.Cancer cell international · 2021Article
- Single-particle analysis of urea amidolyase reveals its molecular mechanism.Protein science : a publication of the Protein Society · 2020Article
- Kinetic, Structural, and Mutational Analysis of Acyl-CoA Carboxylase FromFrontiers in molecular biosciences · 2020Article
- Article
- Crystal structure of the essential biotin-dependent carboxylase AccA3 fromFEBS open bio · 2017Article
- SIRT4 Is a Lysine Deacylase that Controls Leucine Metabolism and Insulin Secretion.Cell metabolism · 2017Article
- A distinct holoenzyme organization for two-subunit pyruvate carboxylase.Nature communications · 2016Article
- The dynamic organization of fungal acetyl-CoA carboxylase.Nature communications · 2016Article
- A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation.Cell discovery · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
3-Methylcrotonyl-CoA carboxylase (MCC), a member of the biotin-dependent carboxylase superfamily, is essential for the metabolism of leucine, and deficient mutations in this enzyme are linked to methylcrotonylglycinuria (MCG) and other serious diseases in humans. MCC has strong sequence conservation with propionyl-CoA carboxylase (PCC), and their holoenzymes are both 750-kilodalton (kDa) α(6)β(6) dodecamers. Therefore the architecture of the MCC holoenzyme is expected to be highly similar to that of PCC. Here we report the crystal structures of the Pseudomonas aeruginosa MCC (PaMCC) holoenzyme, alone and in complex with coenzyme A. Surprisingly, the structures show that the architecture and overall shape of PaMCC are markedly different when compared to PCC. The α-subunits show trimeric association in the PaMCC holoenzyme, whereas they have no contacts with each other in PCC. Moreover, the positions of the two domains in the β-subunit of PaMCC are swapped relative to those in PCC. This structural information establishes a foundation for understanding the disease-causing mutations of MCC and provides new insights into the catalytic mechanism and evolution of biotin-dependent carboxylases. The large structural differences between MCC and PCC also have general implications for the relationship between sequence conservation and structural similarity.
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.