Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris
c-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-GM...
| Main Authors: | , , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
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2013
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| Online Access: | https://hdl.handle.net/10356/95551 http://hdl.handle.net/10220/9183 |
| _version_ | 1826125394552553472 |
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| author | Liao, Yi-Ting Chin, Ko-Hsin Kuo, Wei-Ting Chuah, Mary Lay-Cheng Liang, Zhao-Xun Chou, Shan-Ho |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Liao, Yi-Ting Chin, Ko-Hsin Kuo, Wei-Ting Chuah, Mary Lay-Cheng Liang, Zhao-Xun Chou, Shan-Ho |
| author_sort | Liao, Yi-Ting |
| collection | NTU |
| description | c-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. |
| first_indexed | 2024-10-01T06:35:55Z |
| format | Journal Article |
| id | ntu-10356/95551 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:35:55Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/955512023-02-28T17:03:48Z Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris Liao, Yi-Ting Chin, Ko-Hsin Kuo, Wei-Ting Chuah, Mary Lay-Cheng Liang, Zhao-Xun Chou, Shan-Ho School of Biological Sciences c-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. Published version 2013-02-20T03:43:23Z 2019-12-06T19:17:06Z 2013-02-20T03:43:23Z 2019-12-06T19:17:06Z 2012 2012 Journal Article Liao, 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. 1744-3091 https://hdl.handle.net/10356/95551 http://hdl.handle.net/10220/9183 10.1107/S1744309112000590 22442228 en Acta crystallographica section F Structural Biology and Crystallization Communications © 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. application/pdf |
| spellingShingle | Liao, Yi-Ting Chin, Ko-Hsin Kuo, Wei-Ting Chuah, Mary Lay-Cheng Liang, Zhao-Xun Chou, Shan-Ho Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris |
| title | Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris |
| title_full | Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris |
| title_fullStr | Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris |
| title_full_unstemmed | Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris |
| title_short | Crystallization and preliminary X-ray diffraction characterization of the XccFimXEAL-c-di-GMP and XccFimXEAL-c-di-GMP-XccPilZ complexes from Xanthomonas campestris |
| title_sort | crystallization and preliminary x ray diffraction characterization of the xccfimxeal c di gmp and xccfimxeal c di gmp xccpilz complexes from xanthomonas campestris |
| url | https://hdl.handle.net/10356/95551 http://hdl.handle.net/10220/9183 |
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