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.
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.
Institute of Biochemistry, National Chung-Hsing University, Taichung 40227, Taiwan.
Tso Ning
TN
Li
Ko Hsin
KH
Chin
Hui Ling
HL
Shih
Andrew H J
AH
Wang
Shan Ho
SH
Chou
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006152:Cyclic GMP / Q000031:analogs & derivatives; D015290:Second Messenger Systems; D016959:Xanthomonas campestris / Q000378:metabolism / Q000472:pathogenicity*
D001426:Bacterial Proteins; C062025:bis(3',5')-cyclic diguanylic acid; D006152:Cyclic GMP