5HY5
Crystal Structure of a Tryptophan 6-halogenase (SttH) from Streptomyces toxytricini
Summary for 5HY5
| Entry DOI | 10.2210/pdb5hy5/pdb |
| Descriptor | Tryptophan 6-halogenase, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | tryptophan halogenase, oxidoreductase |
| Biological source | Streptomyces toxytricini |
| Total number of polymer chains | 2 |
| Total formula weight | 119218.25 |
| Authors | Levy, C. (deposition date: 2016-02-01, release date: 2016-02-17, Last modification date: 2024-05-01) |
| Primary citation | Shepherd, S.A.,Menon, B.R.,Fisk, H.,Struck, A.W.,Levy, C.,Leys, D.,Micklefield, J. A Structure-Guided Switch in the Regioselectivity of a Tryptophan Halogenase. Chembiochem, 17:821-824, 2016 Cited by PubMed Abstract: Flavin-dependent halogenases are potentially useful biocatalysts for the regioselective halogenation of aromatic compounds. Haloaromatic compounds can be utilised in the synthesis and biosynthesis of pharmaceuticals and other valuable products. Here we report the first X-ray crystal structure of a tryptophan 6-halogenase (SttH), which enabled key residues that contribute to the regioselectivity in tryptophan halogenases to be identified. Structure-guided mutagenesis resulted in a triple mutant (L460F/P461E/P462T) that exhibited a complete switch in regioselectivity; with the substrate 3-indolepropionate 75 % 5-chlorination was observed with the mutant in comparison to 90 % 6-chlorination for the wild-type SttH. This is the first clear example of how regiocomplementary halogenases can be created from a single parent enzyme. The biocatalytic repertoire of SttH was also expanded to include a range of indolic and non-indolic substrates. PubMed: 26840773DOI: 10.1002/cbic.201600051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.68 Å) |
Structure validation
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