9mc1

Trans-acting enoylreductase PhiaB involved in the phialotideA biosynthesis pathway

spinqualitylabelsall models 9mc1, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9mc1 is a 1 chain structure with sequence from Pseudophialophora. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Fungal polyketides are diverse natural products synthesized by iterative polyketide synthases (i-PKSs) and modified by enzymes such as trans-acting enoylreductases (trans-ERs). In this study, we investigated PhiaB and PhomB, trans-ERs involved in the biosynthesis of polyhydroxy polyketides, phialotides, and phomenoic acids. In vitro assays using substrate analogs revealed distinct chain-length preferences. X-ray structural analysis of PhiaB revealed distinct N-terminal, central, and C-terminal regions. The importance of the central region, which possesses a canonical Rossmann fold for cofactor recognition, was further supported by biosynthetic refactoring using a chimeric enzyme. Docking studies revealed key amino acid residues that may be involved in substrate/cofactor recognition. These findings advance our understanding of trans-ER function, providing opportunities for the synthesis of structurally different polyhydroxy polyketides by genetic engineering of polyhydroxy polyketide biosynthesis. Chain-length preference of trans-acting enoylreductases involved in the biosynthesis of fungal polyhydroxy polyketides.,Takekawa Y, Takino J, Sato S, Oikawa H, Ose T, Minami A Biochem Biophys Res Commun. 2025 May 1;761:151737. doi: , 10.1016/j.bbrc.2025.151737. Epub 2025 Apr 1. PMID:40186921 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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