Structural and biochemical characterization of the yeast HD domain containing protein YGK1 reveals a metal-dependent nucleoside 5 '-monophosphatase
文献类型：期刊论文
| 作者 | Liu, QS ; Yang, JS; Wang F(王飞); Zhou K(周柯); Gao ZQ(高增强); 刘鹏(多); Dong YH(董宇辉); Liu QS(刘全胜); Wang, F; Yang, D
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| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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| 出版日期 | 2018 |
| 卷号 | 501期号:3页码:674-681 |
| ISSN号 | 0006-291X |
| 关键词 | HD domain containing protein 5 ' nucleotidase Dimerization Nucleoside 5 ' Monophosphate |
| DOI | 10.1016/j.bbrc.2018.05.047 |
| 文献子类 | Article |
| 英文摘要 | HD-domain is a conserved domain, with the signature of histidine and aspartic (HD) residues doublets. HD-domain proteins may possess nucleotidase and phosphodiesterase activities, and they play important roles in signaling and nucleotide metabolism. In yeast, HD-domain proteins with nucleotidase activity remained unexplored. Here, we biochemically and structurally characterized two HD domain proteins YGK1 (YGL101W) and YB92 (YBR242W) from Saccharomyces cerevisiae as nucleoside 5'-monophosphatases, with substrate preference for deoxyribonucleoside 5'-monophosphatase over ribonucleoside 5'-monophosphatase. By determining the crystal structure of YGKI, we unveiled that YGKI structure resembled as the crystal structure of YfbR from E. coli. Size-exclusion chromatography and crosslinking studies suggested that YGKI and YB92 existed in the form of a dimer, respectively, which were consistent with structural observation of YGKI. Site-directed mutagenesis demonstrated that more extensive conserved residues near the divalent metal coordinating active site were essential for YGK1 activity than previous suggested. The metal coordinating His89 and Asp90, and the neighboring conserved Glu93, Glu114 and Glu145 were individually critical for catalysis. In addition, alignments suggested that three flexible loops with hydrophobic residues might be implicated in substrate selectivity to nucleoside moiety. Together, our comparative structural and mutational studies suggested that YGK1 and YB92 functioned as 5'-nucleotidases in S. cerevisiae. (C) 2018 Elsevier Inc. All rights reserved. |
| 电子版国际标准刊号 | 1090-2104 |
| WOS关键词 | ESCHERICHIA-COLI ; 5'-NUCLEOTIDASES ; NUCLEOTIDASES ; PHOSPHOHYDROLASE ; PHOSPHATASE ; YJJG ; YFBR |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000436057500011 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/286057]  |
| 专题 | 高能物理研究所_多学科研究中心 高能物理研究所_实验物理中心 |
| 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 | Liu, QS,Yang, JS,Wang F,et al. Structural and biochemical characterization of the yeast HD domain containing protein YGK1 reveals a metal-dependent nucleoside 5 '-monophosphatase[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2018,501(3):674-681. |
| APA | Liu, QS.,Yang, JS.,王飞.,周柯.,高增强.,...&Zhang, JJ.(2018).Structural and biochemical characterization of the yeast HD domain containing protein YGK1 reveals a metal-dependent nucleoside 5 '-monophosphatase.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,501(3),674-681. |
| MLA | Liu, QS,et al."Structural and biochemical characterization of the yeast HD domain containing protein YGK1 reveals a metal-dependent nucleoside 5 '-monophosphatase".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 501.3(2018):674-681. |
入库方式： OAI收割
来源：高能物理研究所
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