Crystallization and preliminary X-ray diffraction characterization of an essential protein from Xanthomonas campestris that contains a noncanonical PilZ signature motif yet is critical for pathogenicity

Tso Ning Li, Ko Hsin Chin, Hui Ling Shih, Andrew H.J. Wang, Shan Ho Chou

研究成果: 雜誌貢獻文章同行評審

4 引文 斯高帕斯(Scopus)

摘要

Recent studies have identified c-di-GMP as a novel secondary messenger molecule that is heavily involved in regulating bacterial biofilm formation, motility, production of pathogenicity factors etc. PilZ domain-containing proteins have been suggested and subsequently proved to be the c - di-GMP receptor. However, considering the diverse biological functions exhibited by c - di-GMP, it may be that receptors other than the PilZ domain exist. An essential protein from the plant pathogen Xanthomonas campestris pv. campestris (Xcc) that contains a noncanonical PilZ signature motif yet is critical for Xcc pathogenicity has been cloned, purified and crystallized. Detailed characterization of this protein may reveal an alternative binding mode of c-di-GMP and allow a more thorough understanding of how c-di-GMP exhibits its diverse effects.

原文英語
頁(從 - 到)1056-1059
頁數4
期刊Acta Crystallographica Section F: Structural Biology and Crystallization Communications
65
發行號10
DOIs
出版狀態已發佈 - 2009
對外發佈

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 遺傳學
  • 凝聚態物理學

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