ArticleProceedings of the National Academy of Sciences of the United States of America2006
Structure of a bacterial pyridoxal 5'-phosphate synthase complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 122 citations in OpenAlex.
- Enhanced microbial production of pyridoxine (Vitamin BSynthetic and systems biotechnology · 2026Article
- A Plasmodium-derived nanoparticle vaccine elicits sterile protection against malaria in mice.Nature microbiology · 2026Article
- Activity Regulation of a Glutamine Amidotransferase Bienzyme Complex by Substrate-Induced Subunit Interface Expansion.ACS catalysis · 2025Article
- Article
- Structure and dynamics of the staphylococcal pyridoxal 5-phosphate synthase complex reveal transient interactions at the enzyme interface.The Journal of biological chemistry · 2024Article
- Catalytic Effects of Active Site Conformational Change in the Allosteric Activation of Imidazole Glycerol Phosphate Synthase.ACS catalysis · 2023Article
- CaviDB: a database of cavities and their features in the structural and conformational space of proteins.Database : the journal of biological databases and curation · 2023Article
- Proteome level analysis of drug-resistantFrontiers in microbiology · 2023Article
- Trapping and structural characterisation of a covalent intermediate in vitamin BRSC chemical biology · 2022Article
- Modeling Catalysis in Allosteric Enzymes: Capturing Conformational Consequences.Topics in catalysis · 2022Article
- Recombinant Expression, Purification and Characterization of Pyridoxal 5'-phosphate Synthase fromIranian journal of biotechnology · 2021Article
- Pan-Genome of NovelMicroorganisms · 2021Article
- Enhancing the production of γ-aminobutyric acid in Escherichia coli BL21 by engineering the enzymes of the regeneration pathway of the coenzyme factor pyridoxal 5'-phosphate.World journal of microbiology & biotechnology · 2021Article
- Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.Nature communications · 2021Article
- Underground metabolism facilitates the evolution of novel pathways for vitamin B6 biosynthesis.Applied microbiology and biotechnology · 2021Review
- Structural Dynamics and Perspectives of Vitamin B6 Biosynthesis Enzymes inFrontiers in cellular and infection microbiology · 2021Review
- Solution Structures and Dynamic Assembly of the 24-Meric Plasmodial Pdx1-Pdx2 Complex.International journal of molecular sciences · 2020Article
- Essential Metabolic Routes as a Way to ESKAPE From Antibiotic Resistance.Frontiers in public health · 2020Article
- A Label-free Mass Spectrometry Method to Predict Endogenous Protein Complex Composition.Molecular & cellular proteomics : MCP · 2019Article
- Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vitamin B6 is an essential metabolic cofactor that has more functions in humans than any other single nutrient. Its de novo biosynthesis occurs through two mutually exclusive pathways that are absent in animals. The predominant pathway found in most prokaryotes, fungi, and plants has only recently been discovered. It is distinguished by a glutamine amidotransferase, which is remarkable in that it alone can synthesize the cofactor form, pyridoxal 5'-phosphate (PLP), directly from a triose and a pentose saccharide and glutamine. Here we report the 3D structure of the PLP synthase complex with substrate glutamine bound as well as those of the individual synthase and glutaminase subunits Pdx1 and Pdx2, respectively. The complex is made up of 24 protein units assembled like a cogwheel, a dodecameric Pdx1 to which 12 Pdx2 subunits attach. In contrast to the architecture of previously determined glutamine amidotransferases, macromolecular assembly is directed by an N-terminal alpha-helix on the synthase. Interaction with the synthase subunit leads to glutaminase activation, resulting in formation of an oxyanion hole, a prerequisite for catalysis. Mutagenesis permitted identification of the remote glutaminase and synthase catalytic centers and led us to propose a mechanism whereby ammonia shuttles between these active sites through a methionine-rich hydrophobic tunnel.
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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.