ArticleStructure (London, England : 1993)2009
A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 64 citations in OpenAlex.
- Hydrolysis of the acetyl-CoA allosteric activator by Staphylococcus aureus pyruvate carboxylase.Archives of biochemistry and biophysics · 2025Article
- Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase.Nature structural & molecular biology · 2025Article
- Analysis of the Antibiotic-Potentiating Activity, Absorption, Distribution, Metabolism, and Excretion (ADME) and the Molecular Docking Properties of Phytol Against Multi-Drug-Resistant (MDR) Strains.Antibiotics (Basel, Switzerland) · 2024Article
- Article
- 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
- Specificity and selectivity in post-translational biotin addition.Biochemical Society transactions · 2018Review
- Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.Nature communications · 2018Article
- Control of biotin biosynthesis in mycobacteria by a pyruvate carboxylase dependent metabolic signal.Molecular microbiology · 2017Article
- c-di-AMP modulates Listeria monocytogenes central metabolism to regulate growth, antibiotic resistance and osmoregulation.Molecular microbiology · 2017Article
- A distinct holoenzyme organization for two-subunit pyruvate carboxylase.Nature communications · 2016Article
- Mechanism of metamifop inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in Echinochloa crus-galli.Scientific reports · 2016Article
- Structure and substrate selectivity of the 750-kDa α6β6 holoenzyme of geranyl-CoA carboxylase.Nature communications · 2015Article
- The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase.Archives of biochemistry and biophysics · 2014Article
- The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function.Cell · 2014Article
- Functional conformations for pyruvate carboxylase during catalysis explored by cryoelectron microscopy.Structure (London, England : 1993) · 2014Article
- A multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina.PloS one · 2014Article
- Insights into the carboxyltransferase reaction of pyruvate carboxylase from the structures of bound product and intermediate analogs.Biochemical and biophysical research communications · 2013Article
- A substrate-induced biotin binding pocket in the carboxyltransferase domain of pyruvate carboxylase.The Journal of biological chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Pyruvate carboxylase (PC) is a conserved metabolic enzyme with important cellular functions. We report crystallographic and cryo-electron microscopy (EM) studies of Staphylococcus aureus PC (SaPC) in complex with acetyl-CoA, an allosteric activator, and mutagenesis, biochemical, and structural studies of the biotin binding site of its carboxyltransferase (CT) domain. The disease-causing A610T mutation abolishes catalytic activity by blocking biotin binding to the CT active site, and Thr908 might play a catalytic role in the CT reaction. The crystal structure of SaPC in complex with CoA reveals a symmetrical tetramer, with one CoA molecule bound to each monomer, and cryo-EM studies confirm the symmetrical nature of the tetramer. These observations are in sharp contrast to the highly asymmetrical tetramer of Rhizobium etli PC in complex with ethyl-CoA. Our structural information suggests that acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of PC that might be catalytically more competent.
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.