a novel tetrameric pilz domain structure from xanthomonads一种新型四聚物的从xanthomonads pilz域结构.pdfVIP

A Novel Tetrameric PilZ Domain Structure from Xanthomonads 1 2 3 3 4 1,5 Tso-Ning Li , Ko-Hsin Chin , Kit-Man Fung , Ming-Te Yang , Andrew H.-J. Wang , Shan-Ho Chou * 1 Institute of Biochemistry, National Chung-Hsing University, Taichung, Taiwan, Republic of China, 2 National Chung-Hsing University Biotechnology Center, National Chung-Hsing University, Taichung, Taiwan, Republic of China, 3 Institute of Molecular Biology, National Chung-Hsing University, Taichung, Taiwan, Republic of China, 4 Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan, Republic of China, 5 Graduate Institute of Basic Medical Science, China Medical University, Taichung, Taiwan, Republic of China Abstract PilZ domain is one of the key receptors for the newly discovered secondary messenger molecule cyclic di-GMP (c-di-GMP). To date, several monomeric PilZ domain proteins have been identified. Some exhibit strong c-di-GMP binding activity, while others have barely detectable c-di-GMP binding activity and require an accessory protein such as FimX to indirectly respond to the c-di-GMP signal. We now report a novel tetrameric PilZ domain structure of XCC6012 from the plant pathogen Xanthomonas campestris pv. campestris (Xcc). It is one of the four PilZ domain proteins essential for Xcc pathogenicity. Although the monomer adopts a structure similar to those of the PilZ domains with very weak c-di-GMP binding activity, it is nevertheless interrupted in the middle by two extra long helices. Four XCC6012 proteins are thus self-assembled into a tetramer via the extra heptad repe