3pkp | pdb_00003pkp

Q83S Variant of S. Enterica RmlA with dATP

spinqualitylabelsall models 3pkp, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pkp is a 8 chain structure with sequence from "bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DTP, MG Related: 1mp3, 1mp4, 1mp5, 1iim, 1iin, 3pkq Gene: rfbA, rmlA, STM2095 ("Bacillus typhimurium" Loeffler 1892) Activity: Glucose-1-phosphate thymidylyltransferase, with EC number 2.7.7.24 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RMLA_SALTY] Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars. Publication Abstract from PubMed Directed evolution is a valuable technique to improve enzyme activity in the absence of a priori structural knowledge, which can be typically enhanced via structure-guided strategies. In this study, a combination of both whole-gene error-prone polymerase chain reaction and site-saturation mutagenesis enabled the rapid identification of mutations that improved RmlA activity toward non-native substrates. These mutations have been shown to improve activities over 10-fold for several targeted substrates, including non-native pyrimidine- and purine-based NTPs as well as non-native d- and l-sugars (both alpha- and beta-isomers). This study highlights the first broadly applicable high throughput sugar-1-phosphate nucleotidyltransferase screen and the first proof of concept for the directed evolution of this enzyme class toward the identification of uniquely permissive RmlA variants. Expanding the Nucleotide and Sugar 1-Phosphate Promiscuity of Nucleotidyltransferase RmlA via Directed Evolution.,Moretti R, Chang A, Peltier-Pain P, Bingman CA, Phillips GN Jr, Thorson JS J Biol Chem. 2011 Apr 15;286(15):13235-43. Epub 2011 Feb 11. PMID:21317292 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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