Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine
文献类型：期刊论文
| 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 |
| 刊名 | acta crystallographica section f-structural biology communications
 |
| 出版日期 | 2015-04-01 |
| 卷号 | 71页码:393-396 |
| 关键词 | Aeromonas hydrophila MtaN-1 S-adenosylmethionine |
| 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. |
| 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 |
| 关键词[WOS] | 5'-methylthioadenosine/s-adenosylhomocysteine nucleosidase ; enzyme ; infection ; catalysis |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000352508000005 |
| 公开日期 | 2016-05-09 |
| 源URL | [http://cas-ir.dicp.ac.cn/handle/321008/146154]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 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 |
| 推荐引用方式 GB/T 7714 | 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. |
| APA | Xu, Yongbin.,Quan, Chun-Shan.,Jin, Xiaoling.,Jin, Xuanzhen.,Zhao, Jing.,...&Ha, Nam-Chul.(2015).Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine.acta crystallographica section f-structural biology communications,71,393-396. |
| MLA | Xu, Yongbin,et al."Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine".acta crystallographica section f-structural biology communications 71(2015):393-396. |
入库方式： OAI收割
来源：大连化学物理研究所
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