ArticleThe Journal of biological chemistry2011
Tyrosine latching of a regulatory gate affords allosteric control of aromatic amino acid biosynthesis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 62 citations in OpenAlex.
- Influence of Cysteine 440 on the Active Site Properties of 3-Deoxy-d-Arabino-Heptulosonate 7-Phosphate Synthase inACS omega · 2023Article
- Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain.The FEBS journal · 2020Article
- A single amino acid substitution uncouples catalysis and allostery in an essential biosynthetic enzyme inThe Journal of biological chemistry · 2020Article
- Coupling dynamics and evolutionary information with structure to identify protein regulatory and functional binding sites.Proteins · 2019Article
- BEES: Bayesian Ensemble Estimation from SAS.Biophysical journal · 2019Article
- Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium.The Journal of biological chemistry · 2019Article
- Hinge Twists and Population Shifts Deliver Regulated Catalysis for ATP-PRT in Histidine Biosynthesis.Biophysical journal · 2019Article
- Domain cross-talk within a bifunctional enzyme provides catalytic and allosteric functionality in the biosynthesis of aromatic amino acids.The Journal of biological chemistry · 2019Article
- Exploring modular allostery via interchangeable regulatory domains.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.Frontiers in molecular biosciences · 2018Review
- Uncoupling conformational states from activity in an allosteric enzyme.Nature communications · 2017Article
- Structure of Chorismate Mutase-like Domain of DAHPS from Bacillus subtilis Complexed with Novel Inhibitor Reveals Conformational Plasticity of Active Site.Scientific reports · 2017Article
- X-ray Scattering Studies of Protein Structural Dynamics.Chemical reviews · 2017Review
- Article
- Interdomain Conformational Changes Provide Allosteric Regulation en Route to Chorismate.The Journal of biological chemistry · 2016Article
- Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Scientific reports · 2016Article
- Article
- First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Functional Unit of Neisseria meningitidis 3-Deoxy-ᴅ-Arabino-Heptulosonate 7-Phosphate Synthase Is Dimeric.PloS one · 2016Article
- Neisseria meningitidis expresses a single 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase that is inhibited primarily by phenylalanine.Protein science : a publication of the Protein Society · 2013Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first step of the shikimate pathway for aromatic amino acid biosynthesis is catalyzed by 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS). Thermotoga maritima DAH7PS (TmaDAH7PS) is tetrameric, with monomer units comprised of a core catalytic (β/α)(8) barrel and an N-terminal domain. This enzyme is inhibited strongly by tyrosine and to a lesser extent by the presence of phenylalanine. A truncated mutant of TmaDAH7PS lacking the N-terminal domain was catalytically more active and completely insensitive to tyrosine and phenylalanine, consistent with a role for this domain in allosteric inhibition. The structure of this protein was determined to 2.0 Å. In contrast to the wild-type enzyme, this enzyme is dimeric. Wild-type TmaDAH7PS was co-crystallized with tyrosine, and the structure of this complex was determined to a resolution of 2.35 Å. Tyrosine was found to bind at the interface between two regulatory N-terminal domains, formed from diagonally located monomers of the tetramer, revealing a major reorganization of the regulatory domain with respect to the barrel relative to unliganded enzyme. This significant conformational rearrangement observed in the crystal structures was also clearly evident from small angle X-ray scattering measurements recorded in the presence and absence of tyrosine. The closed conformation adopted by the protein on tyrosine binding impedes substrate entry into the neighboring barrel, revealing an unusual tyrosine-controlled gating mechanism for allosteric control of this enzyme.
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