2p6p | pdb_00002p6p
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X-ray crystal structure of C-C bond-forming dTDP-D-Olivose-transferase UrdGT2
Overview
The glycosyltransferase UrdGT2 from Streptomyces fradiae catalyzes the, formation of a glycosidic C-C bond between a polyketide aglycone and, D-olivose. The enyzme was expressed in Escherichia coli, purified and, crystallized. Its structure was established by X-ray diffraction at 1.9 A, resolution. It is the first structure of a C-glycosyltransferase. UrdGT2, belongs to the structural family GT-B of the glycosyltransferases and is, likely to form a C(2)-symmetric dimer in solution. The binding structures, of donor and acceptor substrates in five structurally homologous enzymes, provided a clear and consistent guide for the substrate-binding structure, in UrdGT2. The modeled substrate locations suggest the deeply buried, Asp137 as the activator for C-C bond formation and explain the reaction., The putative model can be used to design mutations that change the, substrate specificity. Such mutants are of great interest in overcoming, the increasing danger of antibiotic resistance.
About this Structure
2P6P is a Protein complex structure of sequences from Streptomyces fradiae with GOL as ligand. Full crystallographic information is available from OCA.
Reference
Structure and Action of the C-C Bond-forming Glycosyltransferase UrdGT2 Involved in the Biosynthesis of the Antibiotic Urdamycin., Mittler M, Bechthold A, Schulz GE, J Mol Biol. 2007 Jun 9;. PMID:17640665
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