8eh1

Engineered tyrosine synthase (TmTyrS1) derived from T. maritima TrpB with Ser bound as the amino-acrylate intermediate and complexed with 4-hydroxyquinoline

spinqualitylabelsall models 8eh1, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8eh1 is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: 0JO, ES1, K Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRPB1_THEMA The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. Publication Abstract from PubMed Aromatic amino acids and their derivatives are diverse primary and secondary metabolites with critical roles in protein synthesis, cell structure and integrity, defense and signaling. All de novo aromatic amino acid production relies on a set of ancient and highly conserved chemistries. Here we introduce a new enzymatic transformation for L-tyrosine synthesis by demonstrating that the beta-subunit of tryptophan synthase-which natively couples indole and L-serine to form L-tryptophan-can act as a latent 'tyrosine synthase'. A single substitution of a near-universally conserved catalytic residue unlocks activity toward simple phenol analogs and yields exclusive para carbon-carbon bond formation to furnish L-tyrosines. Structural and mechanistic studies show how a new active-site water molecule orients phenols for a nonnative mechanism of alkylation, with additional directed evolution resulting in a net >30,000-fold rate enhancement. This new biocatalyst can be used to efficiently prepare valuable L-tyrosine analogs at gram scales and provides the missing chemistry for a conceptually different pathway to L-tyrosine. The beta-subunit of tryptophan synthase is a latent tyrosine synthase.,Almhjell PJ, Johnston KE, Porter NJ, Kennemur JL, Bhethanabotla VC, Ducharme J, Arnold FH Nat Chem Biol. 2024 May 14. doi: 10.1038/s41589-024-01619-z. PMID:38744987 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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