5IXJ
Tryptophan Synthase beta-subunit from Pyrococcus furiosus with L-threonine non-covalently bound in the active site
Summary for 5IXJ
| Entry DOI | 10.2210/pdb5ixj/pdb |
| Descriptor | Tryptophan synthase beta chain 1, THREONINE, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | substrate analog, lyase, plp, fold-type ii |
| Biological source | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Total number of polymer chains | 4 |
| Total formula weight | 176108.62 |
| Authors | Buller, A.R.,Herger, M.,Arnold, F.H. (deposition date: 2016-03-23, release date: 2016-08-17, Last modification date: 2023-11-15) |
| Primary citation | Herger, M.,van Roye, P.,Romney, D.K.,Brinkmann-Chen, S.,Buller, A.R.,Arnold, F.H. Synthesis of beta-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase. J.Am.Chem.Soc., 138:8388-8391, 2016 Cited by PubMed Abstract: We report that l-threonine may substitute for l-serine in the β-substitution reaction of an engineered subunit of tryptophan synthase from Pyrococcus furiosus, yielding (2S,3S)-β-methyltryptophan (β-MeTrp) in a single step. The trace activity of the wild-type β-subunit on this substrate was enhanced more than 1000-fold by directed evolution. Structural and spectroscopic data indicate that this increase is correlated with stabilization of the electrophilic aminoacrylate intermediate. The engineered biocatalyst also reacts with a variety of indole analogues and thiophenol for diastereoselective C-C, C-N, and C-S bond-forming reactions. This new activity circumvents the 3-enzyme pathway that produces β-MeTrp in nature and offers a simple and expandable route to preparing derivatives of this valuable building block. PubMed: 27355405DOI: 10.1021/jacs.6b04836 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
Download full validation report
