ArticleStructure (London, England : 1993)2010
Cryo-EM analysis reveals new insights into the mechanism of action of pyruvate carboxylase.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 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
- Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.Nature communications · 2018Article
- 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
- Functional conformations for pyruvate carboxylase during catalysis explored by cryoelectron microscopy.Structure (London, England : 1993) · 2014Article
- A substrate-induced biotin binding pocket in the carboxyltransferase domain of pyruvate carboxylase.The Journal of biological chemistry · 2013Article
- Structure and function of biotin-dependent carboxylases.Cellular and molecular life sciences : CMLS · 2013Review
- Roles of Arg427 and Arg472 in the binding and allosteric effects of acetyl CoA in pyruvate carboxylase.Biochemistry · 2012Article
- Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA.Archives of biochemistry and biophysics · 2012Review
- An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase.Nature · 2011Article
- The ATP-grasp enzymes.Bioorganic chemistry · 2011Review
- Activation and inhibition of pyruvate carboxylase from Rhizobium etli.Biochemistry · 2011Article
- Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli.Biochemistry · 2011Article
- Quaternary structure of the oxaloacetate decarboxylase membrane complex and mechanistic relationships to pyruvate carboxylases.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Pyruvate carboxylase (PC) is a conserved multifunctional enzyme linked to important metabolic diseases. PC homotetramer is arranged in two layers with two opposing monomers per layer. Cryo-EM explores the conformational variability of PC in the presence of different substrates. The results demonstrate that the biotin-carboxyl carrier protein (BCCP) domain localizes near the biotin carboxylase (BC) domain of its own monomer and travels to the carboxyltransferase (CT) domain of the opposite monomer. All density maps show noticeable conformational differences between layers, mainly for the BCCP and BC domains. This asymmetry may be indicative of a coordination mechanism where monomers from different layers catalyze the BC and CT reactions consecutively. A conformational change of the PC tetramerization (PT) domain suggests a new functional role in communication. A long-range communication pathway between subunits in different layers, via interacting PT-PT and BC-BC domains, may be responsible for the cooperativity of PC from Staphylococcus aureus.
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