کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10755603 | 1050376 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Crystal structure and biochemical studies of Brucella melitensis 5â²-methylthioadenosine/S-adenosylhomocysteine nucleosidase
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کلمات کلیدی
PDBMTANr.m.s.d.2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chlorideintS-adenosylhomocysteineMTASAH5′-methylthioadenosine - 5'-methylthioadenosineBrucella - بروسلا SeMet - خودشانCrystal structure - ساختار کریستالیseleno-methionine - سلنو متیونینSAD - غمگینroot mean square deviation - میانگین انحراف مربع ریشهwild-type - نوع وحشیsingle-wavelength anomalous diffraction - پراش ناهمواری تک طول موجProtein Data Bank - پروتئین بانک اطلاعاتیpolyethylene glycol - پلی اتیلن گلیکولPEG - پلیاتیلن گلیکول
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Crystal structure and biochemical studies of Brucella melitensis 5â²-methylthioadenosine/S-adenosylhomocysteine nucleosidase Crystal structure and biochemical studies of Brucella melitensis 5â²-methylthioadenosine/S-adenosylhomocysteine nucleosidase](/preview/png/10755603.png)
چکیده انگلیسی
The prokaryotic 5â²-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) catalyzes the irreversible cleavage of the glycosidic bond in 5â²-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH), a process that plays a key role in several metabolic pathways. Its absence in all mammalian species has implicated this enzyme as a promising target for antimicrobial drug design. Here, we report the crystal structure of BmMTAN in complex with its product adenine at a resolution of 2.6Â Ã
determined by single-wavelength anomalous dispersion method. 11 key residues were mutated for kinetic characterization. Mutations of Tyr134 and Met144 resulted in the largest overall increase in Km, whereas mutagenesis of residues Glu18, Glu145 and Asp168 completely abolished activity. Glu145 and Asp168 were identified as active site residues essential for catalysis. The catalytic mechanism and implications of this structure for broad-based antibiotic design are discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 446, Issue 4, 18 April 2014, Pages 965-970
Journal: Biochemical and Biophysical Research Communications - Volume 446, Issue 4, 18 April 2014, Pages 965-970
نویسندگان
Xusheng Kang, Yan Zhao, Daohua Jiang, Xuemei Li, Xianping Wang, Yan Wu, Zeliang Chen, Xuejun C. Zhang,