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7DMB

Crystal structure of trans-methyltransferase CalH complex with SAH

Summary for 7DMB
Entry DOI10.2210/pdb7dmb/pdb
DescriptorPutative methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
Functional Keywordsmethyltransferase, calh, calbistrin a biosynthesis, transferase
Biological sourceEmericella variicolor
Total number of polymer chains2
Total formula weight87657.08
Authors
Tao, H.,Mori, T.,Abe, I. (deposition date: 2020-12-03, release date: 2021-02-10, Last modification date: 2024-03-27)
Primary citationTao, 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: 33480463
DOI: 10.1002/anie.202016525
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

226707

数据于2024-10-30公开中

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