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Mechanism of the allosteric regulation of Streptococcus mutans 2 '-deoxycytidylate deaminase
Li YH(李艳华); Gao ZQ(高增强); Li, YH; Guo, Z; Jin, L; Wang, DQ; Gao, ZQ; Su, XD; Hou, HF; Dong, YH; Dong YH(董宇辉)
2016
发表期刊ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷号72期号:7页码:883-891
通讯作者董宇辉
摘要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 angstrom 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.
文章类型期刊论文
关键词allosteric regulation crystal structure enzyme inactivation enzyme mechanism enzyme structure 2 '-deoxycytidylate deaminase Streptococcus mutans
DOI10.1107/S2059798316009153
关键词[WOS]HUMAN DEOXYCYTIDYLATE DEAMINASE ; HEPATITIS-B-VIRUS ; CYTIDINE DEAMINASE ; CRYSTAL-STRUCTURE ; DNTP POOLS ; SUBSTRATE ; INHIBITOR ; SUBUNIT ; COMPLEX ; BINDING
语种英语
WOS类目Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography
WOS记录号WOS:000379912500007
引用统计
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/260448
专题多学科研究中心
作者单位中国科学院高能物理研究所
推荐引用方式
GB/T 7714
Li YH,Gao ZQ,Li, YH,et al. Mechanism of the allosteric regulation of Streptococcus mutans 2 '-deoxycytidylate deaminase[J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,2016,72(7):883-891.
APA 李艳华.,高增强.,Li, YH.,Guo, Z.,Jin, L.,...&董宇辉.(2016).Mechanism of the allosteric regulation of Streptococcus mutans 2 '-deoxycytidylate deaminase.ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,72(7),883-891.
MLA 李艳华,et al."Mechanism of the allosteric regulation of Streptococcus mutans 2 '-deoxycytidylate deaminase".ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 72.7(2016):883-891.
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