5YDL

The crystal structure of the Acyl Transferase domain of SpnD complex with 2-(pent-4-yn-1-yl)malonyl

Summary for 5YDL

• Entry DOI: 10.2210/pdb5ydl/pdb
• Descriptor: PKS, (2R)-2-methanoylhept-6-ynoic acid (3 entities in total)
• Functional Keywords: pks, acyl transferase domain, transferase
• Biological source: Streptomyces sp. CNQ431
• Total number of polymer chains: 1
• Total formula weight: 46402.61

Authors

Li, Y.,Qu, X.D.,Zhou, J.H. (deposition date: 2017-09-13, release date: 2018-05-23, Last modification date: 2024-10-23)

Primary citation

Li, Y.,Zhang, W.,Zhang, H.,Tian, W.Y.,Wu, L.,Wang, S.W.,Zheng, M.M.,Zhang, J.R.,Sun, C.H.,Deng, Z.X.,Sun, Y.H.,Qu, X.D.,Zhou, J.H.
Structural Basis of a Broadly Selective Acyltransferase from the Polyketide Synthase of Splenocin.
Angew. Chem. Int. Ed. Engl., 57:5823-5827, 2018

PubMed Abstract: 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.

PubMed: 29536601
DOI: 10.1002/anie.201802805

Experimental method

X-RAY DIFFRACTION (2.402 Å)