3IA7
Crystal Structure of CalG4, the Calicheamicin Glycosyltransferase
Summary for 3IA7
| Entry DOI | 10.2210/pdb3ia7/pdb |
| Related | 3IAA |
| Descriptor | CalG4, CALCIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | glycosysltransferase, calicheamicin, calg4, enediyne, transferase |
| Biological source | Micromonospora echinospora (Micromonospora purpurea) |
| Total number of polymer chains | 2 |
| Total formula weight | 88965.20 |
| Authors | Chang, A.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips Jr., G.N. (deposition date: 2009-07-13, release date: 2010-06-02, Last modification date: 2024-11-27) |
| Primary citation | Chang, A.,Singh, S.,Helmich, K.E.,Goff, R.D.,Bingman, C.A.,Thorson, J.S.,Phillips, G.N. Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity. Proc.Natl.Acad.Sci.USA, 108:17649-17654, 2011 Cited by PubMed Abstract: Glycosyltransferases are useful synthetic catalysts for generating natural products with sugar moieties. Although several natural product glycosyltransferase structures have been reported, design principles of glycosyltransferase engineering for the generation of glycodiversified natural products has fallen short of its promise, partly due to a lack of understanding of the relationship between structure and function. Here, we report structures of all four calicheamicin glycosyltransferases (CalG1, CalG2, CalG3, and CalG4), whose catalytic functions are clearly regiospecific. Comparison of these four structures reveals a conserved sugar donor binding motif and the principles of acceptor binding region reshaping. Among them, CalG2 possesses a unique catalytic motif for glycosylation of hydroxylamine. Multiple glycosyltransferase structures in a single natural product biosynthetic pathway are a valuable resource for understanding regiospecific reactions and substrate selectivities and will help future glycosyltransferase engineering. PubMed: 21987796DOI: 10.1073/pnas.1108484108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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