ArticleStructure (London, England : 1993)2014
Functional conformations for pyruvate carboxylase during catalysis explored by cryoelectron microscopy.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Allosteric Site at the Biotin Carboxylase Dimer Interface Mediates Activation and Inhibition inBiochemistry · 2023Article
- CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.Nature communications · 2022Article
- Conformational Selection Governs Carrier Domain Positioning inBiochemistry · 2022Article
- Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.Nature communications · 2018Article
- Roles of pyruvate carboxylase in human diseases: from diabetes to cancers and infection.Journal of molecular medicine (Berlin, Germany) · 2018Review
- Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure and substrate selectivity of the 750-kDa α6β6 holoenzyme of geranyl-CoA carboxylase.Nature communications · 2015Article
- The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function.Cell · 2014Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The tetrameric enzyme pyruvate carboxylase (PC), a biotin-dependent carboxylase, produces oxaloacetate by two consecutive reactions that take place in distant active sites. Previous crystal structures revealed two different configurations for PC tetramers, the so-called symmetric and asymmetric, which were understood as characteristic molecular architectures for PC from different organisms. We have analyzed PC samples from Staphylococcus aureus while the enzyme generates oxaloacetate, expecting PC tetramers to display the conformational landscape relevant for its functioning. Using cryoelectron microscopy (cryo-EM) and sorting techniques, we detect previously defined symmetric and asymmetric architectures, demonstrating that PC maps both arrangements by large conformational changes. Furthermore, we observe that each configuration is coupled to one of the two consecutive enzymatic reactions. The findings describe the structural transitions relevant for the allosteric control of the multifunctional PC and demonstrate that by cryo-EM and classification, we can characterize freely working macromolecules.
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