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题名: Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine
作者: Xu, Yongbin1, 2;  Quan, Chun-Shan1;  Jin, Xiaoling1;  Jin, Xuanzhen3;  Zhao, Jing1;  Jin, Liming1;  Kim, Jin-Sik4;  Guo, Jianyun1;  Fan, Shengdi1;  Ha, Nam-Chul4
关键词: Aeromonas hydrophila ;  MtaN-1 ;  S-adenosylmethionine
刊名: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
发表日期: 2015-04-01
DOI: 10.1107/S2053230X15003647
卷: 71, 页:393-396
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine ;  Physical Sciences
类目[WOS]: Biochemical Research Methods ;  Biochemistry & Molecular Biology ;  Biophysics ;  Crystallography
研究领域[WOS]: Biochemistry & Molecular Biology ;  Biophysics ;  Crystallography
英文摘要: Prokaryotic 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MtaN) is a multifunctional enzyme that can hydrolyze S-adenosyl-L-homocysteine (SAH) and S-methyl-5'-thioadenosine (MTA) to give S-ribosyl-L-homocysteine (SRH) and S-methyl-5'-thioribose (MTR), respectively. This reaction plays a key role in several metabolic pathways, including biological methylation, polyamine biosynthesis, methionine recycling and bacterial quorum sensing. Structurally, MtaN belongs to the MtnN subfamily of the purine nucleoside phosphorylase (PNP)/uridine phosphorylase (UDP) phosphorylase family. Aeromonas hydrophila has two MtnN subfamily proteins: MtaN-1, a periplasmic protein with an N-terminal signal sequence, and MtaN-2, a cytosolic protein. In this study, MtaN-1 from Aeromonas hydrophila was successfully expressed and purified using Ni-NTA affinity, Q anion-exchange and gel-filtration chromatography. Crystals of the protein in complex with the substrate SAH were obtained and diffracted to a resolution of 1.4 angstrom. The crystals belonged to the trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 102.7, c = 118.8 angstrom. The asymmetric unit contained two molecules of MtaN-1 complexed with SAH.
关键词[WOS]: 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE ;  ENZYME ;  INFECTION ;  CATALYSIS
语种: 英语
WOS记录号: WOS:000352508000005
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/146154
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Dalian Nationalities Univ, Coll Life Sci, Dept Bioengn, Dalian 116600, Peoples R China
2.Chinese Acad Sci, Dalian Inst Chem Phys, Lab Biomed Mat Engn, Dalian 116023, Peoples R China
3.Yanbian Univ, Coll Engn, Yanji 133002, Jilin, Peoples R China
4.Seoul Natl Univ, Coll Agr & Life Sci, Dept Agr Biotechnol, Seoul 151742, South Korea

Recommended Citation:
Xu, Yongbin,Quan, Chun-Shan,Jin, Xiaoling,et al. Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine[J]. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS,2015,71:393-396.
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