1iin
thymidylyltransferase complexed with UDP-glucose
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OverviewOverview
Metabolite glycosylation is affected by three classes of enzymes:, nucleotidylyltransferases, which activate sugars as nucleotide, diphospho-derivatives, intermediate sugar-modifying enzymes and, glycosyltransferases, which transfer the final derivatized activated, sugars to aglycon substrates. One of the first crystal structures of an, enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from, Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is, reported at 2.0 A and 2.1 A resolution, respectively. These structures, in, conjunction with the kinetic characterization of Ep, clarify the catalytic, mechanism of this important enzyme class. Structure-based engineering of, Ep produced modified enzymes capable of utilizing 'unnatural' sugar, phosphates not accepted by wild type Ep. The demonstrated ability to alter, nucleotidylyltransferase specificity by design is an integral component of, in vitro glycosylation systems developed for the production of diverse, glycorandomized libraries.
About this StructureAbout this Structure
1IIN is a Single protein structure of sequence from Salmonella enterica with UPG as ligand. Active as Glucose-1-phosphate thymidylyltransferase, with EC number 2.7.7.24 Full crystallographic information is available from OCA.
ReferenceReference
Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization., Barton WA, Lesniak J, Biggins JB, Jeffrey PD, Jiang J, Rajashankar KR, Thorson JS, Nikolov DB, Nat Struct Biol. 2001 Jun;8(6):545-51. PMID:11373625
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