6zyk | pdb_00006zyk

Non-heme monooxygenase, ThoJ-Ni complex

spinqualitylabelsall models 6zyk, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zyk is a 1 chain structure with sequence from Streptomyces malaysiense. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Ligands: NI, TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1J4PXK4_9ACTN Publication Abstract from PubMed 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 beta-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 thoJ, encoding a predicted nonheme monooxygenase, shows that ThoJ is essential for thioholgamide beta-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. Non-Heme Monooxygenase ThoJ Catalyzes Thioholgamide beta-Hydroxylation.,Sikandar A, Lopatniuk M, Luzhetskyy A, Koehnke J ACS Chem Biol. 2020 Oct 1. doi: 10.1021/acschembio.0c00637. PMID:32965102 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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