3OTH

Crystal Structure of CalG1, Calicheamicin Glycostyltransferase, TDP and calicheamicin alpha3I bound form

Summary for 3OTH

• Entry DOI: 10.2210/pdb3oth/pdb
• Related: 3D0Q 3D0R 3OTG 3OTI
• Descriptor: CalG1, THYMIDINE-5'-DIPHOSPHATE, Calicheamicin alpha3I, ... (4 entities in total)
• Functional Keywords: calicheamicin, tdp, structural genomics, psi-2, protein structure initiative, center for eukaryotic structural genomics, cesg, gt-b fold, glycosyltransferase, transferase-antibiotic complex, enzyme discovery for natural product biosynthesis, natpro, transferase/antibiotic
• Biological source: Micromonospora echinospora (Micromonospora purpurea)
• Total number of polymer chains: 2
• Total formula weight: 90696.07

Authors

Chang, A.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG),Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2010-09-11, release date: 2010-12-15, Last modification date: 2024-11-20)

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

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: 21987796
DOI: 10.1073/pnas.1108484108

Experimental method

X-RAY DIFFRACTION (2.301 Å)