DICP OpenIR
Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine
Xu, Yongbin1,2; Quan, Chun-Shan1; Jin, Xiaoling1; Jin, Xuanzhen3; Zhao, Jing1; Jin, Liming1; Kim, Jin-Sik4; Guo, Jianyun1; Fan, Shengdi1; Ha, Nam-Chul4
KeywordAeromonas Hydrophila Mtan-1 S-adenosylmethionine
Source PublicationACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
2015-04-01
DOI10.1107/S2053230X15003647
Volume71Pages:393-396
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
WOS SubjectBiochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography
WOS Research AreaBiochemistry & Molecular Biology ; Biophysics ; Crystallography
WOS Keyword5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE ; ENZYME ; INFECTION ; CATALYSIS
AbstractProkaryotic 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.
Language英语
WOS IDWOS:000352508000005
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/146154
Collection中国科学院大连化学物理研究所
Affiliation1.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
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.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Xu, Yongbin]'s Articles
[Quan, Chun-Shan]'s Articles
[Jin, Xiaoling]'s Articles
Baidu academic
Similar articles in Baidu academic
[Xu, Yongbin]'s Articles
[Quan, Chun-Shan]'s Articles
[Jin, Xiaoling]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Xu, Yongbin]'s Articles
[Quan, Chun-Shan]'s Articles
[Jin, Xiaoling]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.