Structural highlights
Publication Abstract from PubMed
Polyketides are a large family of pharmaceutically important natural products, and the structural modification of their scaffolds is significant for drug development. Herein, we report high-resolution X-ray crystal structures of the broadly selective acyltransferase (AT) from the splenocin polyketide synthase (SpnD-AT) in the apo form and in complex with benzylmalonyl and pentynylmalonyl extender unit mimics. These structures revealed the molecular basis for the stereoselectivity and substrate specificity of SpnD-AT, and enabled the engineering of the industrially important Ery-AT6 to broaden its substrate scope to include three new types of extender units.
Structural Basis of a Broadly Selective Acyltransferase from the Polyketide Synthase of Splenocin.,Li Y, Zhang W, Zhang H, Tian W, Wu L, Wang S, Zheng M, Zhang J, Sun C, Deng Z, Sun Y, Qu X, Zhou J Angew Chem Int Ed Engl. 2018 May 14;57(20):5823-5827. doi:, 10.1002/anie.201802805. Epub 2018 Apr 14. PMID:29536601[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li Y, Zhang W, Zhang H, Tian W, Wu L, Wang S, Zheng M, Zhang J, Sun C, Deng Z, Sun Y, Qu X, Zhou J. Structural Basis of a Broadly Selective Acyltransferase from the Polyketide Synthase of Splenocin. Angew Chem Int Ed Engl. 2018 May 14;57(20):5823-5827. doi:, 10.1002/anie.201802805. Epub 2018 Apr 14. PMID:29536601 doi:http://dx.doi.org/10.1002/anie.201802805