Mechanism of the allosteric regulation of Streptococcus mutans 2   &apos;-deoxycytidylate deaminase

doi:10.1107/S2059798316009153

CORC > 北京大学 > 生命科学学院

	Mechanism of the allosteric regulation of Streptococcus mutans 2 '-deoxycytidylate deaminase
	Li, Yanhua ; Guo, Zhen ; Jin, Li ; Wang, Deqiang ; Gao, Zengqiang ; Su, Xiaodong ; Hou, Haifeng ; Dong, Yuhui
刊名	ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
	2016
关键词	allosteric regulation crystal structure enzyme inactivation enzyme mechanism enzyme structure 2 &apos Streptococcus mutans HUMAN DEOXYCYTIDYLATE DEAMINASE HEPATITIS-B-VIRUS CYTIDINE DEAMINASE CRYSTAL-STRUCTURE DNTP POOLS SUBSTRATE INHIBITOR SUBUNIT COMPLEX BINDING -deoxycytidylate deaminase
DOI	10.1107/S2059798316009153
英文摘要	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.; National Natural Science Foundation of China [31300622]; Strategic Priority Research Program of the Chinese Academy of Sciences [XDB08030103]; National Basic Research Program of China [2012CB917203]; SCI(E); PubMed; ARTICLE; houhf@ihep.ac.cn; dongyh@ihep.ac.cn; 7; 883-891; 72
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/492028]
专题	生命科学学院
推荐引用方式 GB/T 7714	Li, Yanhua,Guo, Zhen,Jin, Li,et al. Mechanism of the allosteric regulation of Streptococcus mutans 2 '-deoxycytidylate deaminase[J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,2016.
APA	Li, Yanhua.,Guo, Zhen.,Jin, Li.,Wang, Deqiang.,Gao, Zengqiang.,...&Dong, Yuhui.(2016).Mechanism of the allosteric regulation of Streptococcus mutans 2 '-deoxycytidylate deaminase.ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY.
MLA	Li, Yanhua,et al."Mechanism of the allosteric regulation of Streptococcus mutans 2 '-deoxycytidylate deaminase".ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2016).