3D0R
Crystal structure of calG3 from Micromonospora echinospora determined in space group P2(1)
Summary for 3D0R
Entry DOI | 10.2210/pdb3d0r/pdb |
Related | 3D0Q |
Descriptor | Protein CalG3, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL (3 entities in total) |
Functional Keywords | calicheamicin synthesis, glycosyltransferase, enediyne antibiotic, transferase |
Biological source | Micromonospora echinospora |
Total number of polymer chains | 2 |
Total formula weight | 86380.08 |
Authors | Bitto, E.,Bingman, C.A.,Wesenberg, G.E.,Phillips Jr., G.N. (deposition date: 2008-05-02, release date: 2008-06-24, Last modification date: 2023-08-30) |
Primary citation | Zhang, C.,Bitto, E.,Goff, R.D.,Singh, S.,Bingman, C.A.,Griffith, B.R.,Albermann, C.,Phillips, G.N.,Thorson, J.S. Biochemical and structural insights of the early glycosylation steps in calicheamicin biosynthesis. Chem.Biol., 15:842-853, 2008 Cited by PubMed Abstract: The enediyne antibiotic calicheamicin (CLM) gamma(1)(I) is a prominent antitumor agent that is targeted to DNA by a novel aryltetrasaccharide comprised of an aromatic unit and four unusual carbohydrates. Herein we report the heterologous expression and the biochemical characterization of the two "internal" glycosyltransferases CalG3 and CalG2 and the structural elucidation of an enediyne glycosyltransferase (CalG3). In conjunction with the previous characterization of the "external" CLM GTs CalG1 and CalG4, this study completes the functional assignment of all four CLM GTs, extends the utility of enediyne GT-catalyzed reaction reversibility, and presents conclusive evidence of a sequential glycosylation pathway in CLM biosynthesis. This work also reveals the common GT-B structural fold can now be extended to include enediyne GTs. PubMed: 18721755DOI: 10.1016/j.chembiol.2008.06.011 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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