1iin | pdb_00001iin

thymidylyltransferase complexed with UDP-glucose

spinqualitylabelsall models 1iin, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1iin is a 4 chain structure with sequence from "bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: UPG Related: 1iim, 1mp3, 1mp4, 1mp5 Activity: Glucose-1-phosphate thymidylyltransferase, with EC number 2.7.7.24 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q9F7K6_SALCE] Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis (By similarity).[RuleBase:RU003706] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucose-1-phosphate thymidylyltransferase 3D structures

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