5c2o

Crystal structure of Streptococcus mutans Deoxycytidylate Deaminase complexed with dTTP

spinqualitylabelsall models 5c2o, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c2o is a 2 chain structure with sequence from Streptococcus mutans UA159. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, TTP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DSE5_STRMU Publication Abstract from PubMed In cells, dUMP is the intermediate precursor of dTTP in its synthesis during deoxynucleotide metabolism. In Gram-positive bacteria and eukaryotes, zinc-dependent deoxycytidylate deaminases (dCDs) catalyze the conversion of dCMP to dUMP. The activity of dCD is allosterically activated by dCTP and inhibited by dTTP. Here, the crystal structure of Streptococcus mutans dCD (SmdCD) complexed with dTTP is presented at 2.35 A resolution, thereby solving the first pair of activator-bound and inhibitor-bound structures from the same species to provide a more definitive description of the allosteric mechanism. In contrast to the dTTP-bound dCD from the bacteriophage S-TIM5 (S-TIM5-dCD), dTTP-bound SmdCD adopts an inactive conformation similar to the apo form. A structural comparison suggests that the distinct orientations of the triphosphate group in S-TIM5-dCD and SmdCD are a result of the varying protein binding environment. In addition, calorimetric data establish that the modulators bound to dCD can be mutually competitively replaced. The results reveal the mechanism underlying its regulator-specific activity and might greatly enhance the understanding of the allosteric regulation of other dCDs. Mechanism of the allosteric regulation of Streptococcus mutans 2'-deoxycytidylate deaminase.,Li Y, Guo Z, Jin L, Wang D, Gao Z, Su X, Hou H, Dong Y Acta Crystallogr D Struct Biol. 2016 Jul;72(Pt 7):883-91. doi:, 10.1107/S2059798316009153. Epub 2016 Jun 23. PMID:27377385 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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