کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5506278 | 1400289 | 2017 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural and biochemical characterization of FabK from Thermotoga maritima
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کلمات کلیدی
FMNNADPRMSDPDBENRFabKEnoyl-ACP reductase - Enoyl-ACP ردوکتازroot-mean-square deviation - انحراف معیار میانگین ریشهBiochemical characterization - خصوصیات بیوشیمیاییCrystal structure - ساختار کریستالیflavin mononucleotide - فلاون مونونوکلئوتیدnicotinamide adenine dinucleotide phosphate - نیکوتین آمید adenine dinucleotide phosphateProtein Data Bank - پروتئین بانک اطلاعاتی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
TM0800 from Thermotoga maritima is one of the hypothetical proteins with unknown function. The crystal structure determined at 2.3Â Ã
resolution reveals a two domain structure: the N-terminal domain forming a barrel and the C-terminal forming a lid. One FMN is bound between the two domains with the phosphate making intricate hydrogen bonds with protein and three tightly bound water molecules, and the isoalloxazine ring packed against the side chains of Met22 and Met276. The structure is almost identical to that of FabK (enoyl-acyl carrier protein (ACP) reductase, ENR II), a key enzyme in bacterial type II fatty-acid biosynthesis that catalyzes the final step in each elongation cycle; and the enzymatic activity confirms that TM0800 is an ENR. Enzymatic activity was almost completely abolished when the helices connecting the barrel and the lid were deleted. Also, the Met276Ala and Ser280Ala mutants showed a significant reduction in enzymatic activity. The crystal structure of Met276Ala mutant at 1.9Â Ã
resolution showed an absence of FMN suggesting that FMN plays a role in catalysis, and Met276 is important in positioning FMN. TmFabK exists as a dimer in both solution and crystal. Together this study provides molecular basis for the catalytic activity of FabK.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 482, Issue 4, 22 January 2017, Pages 968-974
Journal: Biochemical and Biophysical Research Communications - Volume 482, Issue 4, 22 January 2017, Pages 968-974
نویسندگان
Byung Hak Ha, Sang Chul Shin, Jin Ho Moon, Gyochang Keum, Chan-Wha Kim, Eunice EunKyeong Kim,