Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95551
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dc.contributor.authorLiao, Yi-Tingen
dc.contributor.authorChin, Ko-Hsinen
dc.contributor.authorKuo, Wei-Tingen
dc.contributor.authorChuah, Mary Lay-Chengen
dc.contributor.authorLiang, Zhao-Xunen
dc.contributor.authorChou, Shan-Hoen
dc.date.accessioned2013-02-20T03:43:23Zen
dc.date.accessioned2019-12-06T19:17:06Z-
dc.date.available2013-02-20T03:43:23Zen
dc.date.available2019-12-06T19:17:06Z-
dc.date.copyright2012en
dc.date.issued2012en
dc.identifier.citationLiao, Y.- T., Chin, K.- H., Kuo, W.- T., Chuah, M. L.- C., Liang, Z.- X., & Chou, S.- H. (2012). Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 68(3), 301-305.en
dc.identifier.issn1744-3091en
dc.identifier.urihttps://hdl.handle.net/10356/95551-
dc.description.abstractc-di-GMP is a major secondary-messenger molecule in regulation of bacterial pathogenesis. Therefore, the c-di-GMP-mediated signal transduction network is of considerable interest. The PilZ domain was the first c-di-GMP receptor to be predicted and identified. However, every PilZ domain binds c-di-GMP with a different binding affinity. Intriguingly, a noncanonical PilZ domain has recently been found to serve as a mediator to link FimXEAL to the PilB or PilT ATPase to control the function of type IV pili (T4P). It is thus essential to determine the structure of the FimXEAL-PilZ complex in order to determine how the binding of c-di-GMP to the FimXEAL domain induces conformational change of the adjoining noncanonical PilZ domain, which may transmit information to PilB or PilT to control T4P function. Here, the preparation and preliminary X-ray diffraction studies of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xcc (Xanthomonas campestris pv. campesteris) are reported. Detailed studies of these complexes may allow a more thorough understanding of how c-di-GMP transmits its effects through the degenerate EAL domain and the noncanonical PilZ domain.en
dc.language.isoenen
dc.relation.ispartofseriesActa crystallographica section F Structural Biology and Crystallization Communicationsen
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/S1744309112000590]. 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
dc.titleCrystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestrisen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1107/S1744309112000590en
dc.description.versionPublished versionen
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