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Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP

หน่วยงาน Nanyang Technological University, Singapore

รายละเอียด

ชื่อเรื่อง : Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP
นักวิจัย : Wang, Yu-Chuan , Chin, Ko-Hsin , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho
คำค้น : -
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2555
อ้างอิง : Wang, Y.- C., Chin, K.- H., Chuah, M. L.- C., Liang, Z.- X., & Chou, S.- H. (2012). Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 68(10), 1247-1250. , 1744-3091 , http://hdl.handle.net/10220/9278 , http://dx.doi.org/10.1107/S1744309112036202
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Acta Crystallographica Section F Structural Biology and Crystallization Communications
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Bacterial polynucleotide phosphorylase (PNPase) is a 3'-5' processive exoribonuclease that participates in mRNA turnover and quality control of rRNA precursors in many bacterial species. It also associates with the RNase E scaffold and other components to form a multi-enzyme RNA degradasome machinery that performs a wider regulatory role in degradation, quality control and maturation of mRNA and noncoding RNA. Several crystal structures of bacterial PNPases, as well as some biological activity studies, have been published. However, how the enzymatic activity of PNPase is regulated is less well understood. Recently, Escherichia coli PNPase was found to be a direct c-di-GMP binding target, raising the possibility that c-di-GMP may participate in the regulation of RNA processing. Here, the successful cloning, purification and crystallization of S1-domain-truncated Xanthomonas campestris PNPase (XcPNPaseΔS1) in the presence of c-di-GMP are reported. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 132.76, b = 128.38, c = 133.01 Å, γ = 93.3°, and diffracted to a resolution of 2.00 Å.

บรรณานุกรม :
Wang, Yu-Chuan , Chin, Ko-Hsin , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho . (2555). Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Wang, Yu-Chuan , Chin, Ko-Hsin , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho . 2555. "Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Wang, Yu-Chuan , Chin, Ko-Hsin , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho . "Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2555. Print.
Wang, Yu-Chuan , Chin, Ko-Hsin , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho . Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2555.