Open AccessCrystallization 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
Author(s) -
Li TsoNing,
Chin KoHsin,
Shih HuiLing,
Wang Andrew H.J.,
Chou ShanHo
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109036239
Subject(s) - xanthomonas campestris , biology , xanthomonas , microbiology and biotechnology , computational biology , genetics , bacteria
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.