7DMB
Crystal structure of trans-methyltransferase CalH complex with SAH
Summary for 7DMB
Entry DOI | 10.2210/pdb7dmb/pdb |
Descriptor | Putative methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total) |
Functional Keywords | methyltransferase, calh, calbistrin a biosynthesis, transferase |
Biological source | Emericella variicolor |
Total number of polymer chains | 2 |
Total formula weight | 87657.08 |
Authors | |
Primary citation | Tao, H.,Mori, T.,Wei, X.,Matsuda, Y.,Abe, I. One Polyketide Synthase, Two Distinct Products: Trans-Acting Enzyme-Controlled Product Divergence in Calbistrin Biosynthesis. Angew.Chem.Int.Ed.Engl., 60:8851-8858, 2021 Cited by PubMed Abstract: Calbistrins are fungal polyketides consisting of the characteristic decalin and polyene moieties. Although the biosynthetic gene cluster of calbistrin A was recently identified, the pathway of calbistrin A biosynthesis has largely remained uninvestigated. Herein, we investigated the mechanism by which the backbone structures of calbistrins are formed, by heterologous and in vitro reconstitution of the biosynthesis and a structural biological study. Intriguingly, our analyses revealed that the decalin and polyene portions of calbistrins are synthesized by the single polyketide synthase (PKS) CalA, with the aid of the trans-acting enoylreductase CalK and the trans-acting C-methyltransferase CalH, respectively. We also determined that the esterification of the two polyketide parts is catalyzed by the acyltransferase CalD. Our study has uncovered a novel dual-functional PKS and thus broadened our understanding of how fungi synthesize diverse polyketide natural products. PubMed: 33480463DOI: 10.1002/anie.202016525 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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