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- 저자 : Liming Shang (검색결과 4 건)
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Crystal structure of the nicotinamidase/pyrazinamidase PncA from <i>Bacillus subtilis</i>
Shang, Fei,Chen, Jinli,Wang, Lulu,Jin, Liming,Zou, Linhai,Bu, Tingting,Dong, Yuesheng,Ha, Nam-Chul,Nam, Ki Hyun,Quan, Chunshan,Xu, Yongbin Elsevier 2018 Biochemical and biophysical research communication Vol.503 No.4
<P><B>Abstract</B></P> <P>The nicotinamidase/pyrazinamidase PncA is a member of a large family of hydrolase enzymes that catalyze the deamination of nicotinamide to nicotinic acid. PncA also functions as a pyrazinamidase in a wide variety of eubacteria and is an essential coenzyme in many cellular redox reactions in living systems. We report the crystal structure of substrate-free PncA from <I>Bacillus subtilis</I> (BsPncA) at 2.0 Å resolution to improve our understanding of the PncA family. The structure of BsPncA consists of an α/β domain and a subdomain. The subdomain of BsPncA has a different conformation than that of PncA enzymes from other organisms. The B-factor analysis revealed a rigid structure of the α/β domain, while the subdomain is highly flexible. Both dimers and tetramers were observed in BsPncA protein crystals, but only dimers were observed in solution. Our results provide useful information that will further enhance our understanding of the molecular functions of PncA family members.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Crystal structure of <I>B. Subtilis</I> PncA consists of an α/β domain and a subdomain. </LI> <LI> The metal-binding site of BsPncA is located at the bottom of a large cavity between the core and the subdomain. </LI> <LI> Zinc ion is pentahedrally coordinated within several highly conserved amino acid residues and one water molecule. </LI> <LI> Both dimers and tetramers were observed in BsPncA protein crystals, but only dimers were observed in solution. </LI> </UL> </P>
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Fei Shang,Jinli Chen,Lulu Wang,Yuanyuan Chen,Jing Lan,Wei Liu,Liming Jin,하남철,Chunshan Quan,Yongbin Xu 한국구조생물학회 2019 Biodesign Vol.7 No.1
Sirtuins are NAD+-dependent deacetylase that are broadly conserved throughout bacteria, archaea, and eukaryotes. Themembers of sirtuins are important in regulating diverse biological pathways, including gene silencing, DNA repair, genomestability, longevity, metabolism, and cell physiology. Sirtuin from Bacillus amyloliquefaciens (BaSrtN) is a particularlyinteresting bacterial Sir2 homologue. In this study, to further understand the function and mechanisms of this protein,BaSrtN was successfully expressed and purified using Ni-NTA affinity, Q anion-exchange, and gel-filtration chromatography. Purified BaSrtN was crystallized and diffracted to the resolution of 1.45 Å. The preliminary crystallographic analysissuggested that BaSrtN crystal belongs to the trigonal space group P31 or P32, with unit-cell parameters of a = b = 90.115and c = 86.306 Å. Size-exclusion chromatography suggested that BaSrtN prefer to exit as monomers in solution.
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Aeromonas hydrophila cytosolic 5’-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtaN-2
Jinli Chen,Fei Shang,Lulu Wang,Wei Liu,Yuanyuan Chen,Jing Lan,Liming Jin,Nam-Chul Ha,Chunshan Quan,Yongbin Xu 한국구조생물학회 2018 Biodesign Vol.6 No.3
5’-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) plays a critical role in diverse pathways in bacterial cells such as biological methylation, polyamine biosynthesis, methionine recycling, and bacterial quorum sensing. It has been known that MtaN catalyzes the hydrolysis of N-ribosidic bond of adenosine-based substrates such as S-adenosyl-L-homocysteine (SAH), S-methyl-5’-thioadenosine (MTA) and 5’-deoxyadenosine (5’-DOA). In Aeromonas hydrophila, there are two MtnN subfamily proteins: MtaN-1, a periplasmic protein with an N-terminal signal peptide; and MtaN-2, a cytosolic protein. In this study, MtaN-2 from A. hydrophila was successfully expressed and purified using Ni-NTA affinity, Q anion-exchange, and gel-filtration chromatography. We first crystallized apo MtaN-2 but it diffracted to a low resolution of 5.1 Å. New crystals suitable for diffraction were obtained by adding 2 mM adenosine, a substrate analog of MtaN-2 during purification process and the crystals diffracted to the resolution of 2.0 Å. The crystals belong to the trigonal space group P31 or P32, with unit-cell parameters of a = b = 74.94 Å and c = 185.21 Å. The asymmetric unit contains four complexes of MtaN-2 with hydrolysis products of adenosine.
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Zhixiong Su,Xinping Ye,Liming Shang 연세대학교의과대학 2019 Yonsei medical journal Vol.60 No.1
Purpose: It is well documented that natural killer (NK) cytotoxicity against hepatocellular carcinoma (HCC) cells is impaired inHCC, which might account for the failure of anti-tumor immune response. miRNAs are considered as important regulators forthe development and functions of NK cells. However, the entire role of miR-506 in NK cells remains far from being addressed. Materials and Methods: The expressions of miR-506 and signal transducer and activator of transcription 3 (STAT3) mRNA in primaryNK cells from HCC patients and healthy controls were detected by quantitative real-time PCR. NK cell cytotoxicity was assessedby CFSE/7AAD cytotoxicity assay and lactate dehydrogenase assay. Luciferase reporter assay, RNA immunoprecipitationassay, and western blot were conducted to confirm the interaction between miR-506 and STAT3. Results: miR-506 expression was downregulated and STAT3 mRNA was upregulated in primary NK cells from HCC patients. PrimaryNK cells from HCC patients showed remarkably reduced cytotoxicity against SMMC7721 or HepG2 cells. NK cell cytotoxicitywas positively correlated with miR-506 expression and negatively correlated with STAT3 mRNA expression. Additionally, miR-506 overexpression enhanced NK cell cytotoxicity against HCC cells, while miR-506 inhibitor showed the reverse effect. Moreover,miR-506 could suppress STAT3 expression by directly targeting 3'-untranslated regions of STAT3. A negative correlation betweenmiR-506 and STAT3 mRNA expression in HCC patients was observed. Mechanistically, overexpressing STAT3 greatly reversedmiR-506-mediated promotion of NK cell cytotoxicity against HCC cells. Conclusion: miR-506 enhanced NK cell cytotoxicity against HCC cells by targeting STAT3, suggesting that modulating miR-506expression maybe a promising approach for enhancing NK cell-based antitumor therapies.
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