6ZYL
non-heme monooxygenase; ThoJ apo
Summary for 6ZYL
| Entry DOI | 10.2210/pdb6zyl/pdb |
| Descriptor | Uncharacterized protein, L(+)-TARTARIC ACID (3 entities in total) |
| Functional Keywords | non-heme deoxygenate, metal binding protein, thoj |
| Biological source | Streptomyces malaysiense |
| Total number of polymer chains | 1 |
| Total formula weight | 33728.45 |
| Authors | Koehnke, J.,Sikandar, A. (deposition date: 2020-08-02, release date: 2020-10-14, Last modification date: 2024-01-31) |
| Primary citation | Sikandar, A.,Lopatniuk, M.,Luzhetskyy, A.,Koehnke, J. Non-Heme Monooxygenase ThoJ Catalyzes Thioholgamide beta-Hydroxylation. Acs Chem.Biol., 15:2815-2819, 2020 Cited by PubMed Abstract: Thioviridamide-like compounds, including thioholgamides, are ribosomally synthesized and post-translationally modified peptide natural products with potent anticancer cell activity and an unprecedented structure. Very little is known about their biosynthesis, and we were intrigued by the β-hydroxy-N1, N3-dimethylhistidinium moiety found in these compounds. Here we report the construction of a heterologous host capable of producing thioholgamide with a 15-fold increased yield compared to the wild-type strain. A knockout of , encoding a predicted nonheme monooxygenase, shows that ThoJ is essential for thioholgamide β-hydroxylation. The crystal structure of ThoJ exhibits a typical mono/dioxygenase fold with conserved key active-site residues. Yet, ThoJ possesses a very large substrate binding pocket that appears suitable to receive a cyclic thioholgamide intermediate for hydroxylation. The improved production of the heterologous host will enable the dissection of the individual biosynthetic steps involved in biosynthesis of this exciting RiPP family. PubMed: 32965102DOI: 10.1021/acschembio.0c00637 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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