dc.contributor.authorWang, Yu-Chuan
dc.contributor.authorChin, Ko-Hsin
dc.contributor.authorChuah, Mary Lay-Cheng
dc.contributor.authorLiang, Zhao-Xun
dc.contributor.authorChou, Shan-Ho
dc.date.accessioned2013-02-27T04:39:00Z
dc.date.available2013-02-27T04:39:00Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationWang, 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.en_US
dc.identifier.issn1744-3091en_US
dc.identifier.urihttp://hdl.handle.net/10220/9278
dc.description.abstractBacterial 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.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesActa Crystallographica Section F Structural Biology and Crystallization Communicationsen_US
dc.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.en_US
dc.titleCrystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMPen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1107/S1744309112036202
dc.description.versionPublished versionen_US


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