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 |
卷 | 65 |
發行號 | 10 |
DOIs | |
出版狀態 | 已發佈 - 2009 |
對外發佈 | 是 |
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