Induced-fit upon ligand binding revealed by crystal structures of the hot-dog fold thioesterase in dynemicin biosynthesis.

Liew, C.W.,  Sharff, A.,  Kotaka, M.,  Kong, R.,  Sun, H.,  Qureshi, I.,  Bricogne, G.,  Liang, Z.,  Lescar, J.

Journal: (2010) J.Mol.Biol. 404: 291-306

PubMed: 20888341  
DOI: 10.1016/j.jmb.2010.09.041  
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PubMed Abstract:
Dynemicins are structurally related 10-membered enediyne natural products isolated from Micromonospora chernisa with potent antitumor and antibiotic activity. The early biosynthetic steps of the enediyne moiety of dynemicins are catalyzed by an iterative polyketide synthase (DynE8) and a thioesterase (DynE7).... [ Read More & Search PubMed Abstracts ]