Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95330
Title: Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP
Authors: Wang, Yu-Chuan
Chin, Ko-Hsin
Chuah, Mary Lay-Cheng
Liang, Zhao-Xun
Chou, Shan-Ho
Issue Date: 2012
Source: 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.
Series/Report no.: Acta Crystallographica Section F Structural Biology and Crystallization Communications
Abstract: 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.
URI: https://hdl.handle.net/10356/95330
http://hdl.handle.net/10220/9278
ISSN: 1744-3091
DOI: 10.1107/S1744309112036202
Rights: © 2012 International Union of Crystallography. This paper was published in Acta Crystallographica Section F Structural Biology and Crystallization Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [http://dx.doi.org/10.1107/S1744309112036202]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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