A novel tetrameric PilZ domain structure from xanthomonads.

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 a...

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Autores principales:	Tso-Ning Li, Ko-Hsin Chin, Kit-Man Fung, Ming-Te Yang, Andrew H-J Wang, Shan-Ho Chou
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6dad3a9b1cfe4e5384f78158ff20c605
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spelling	oai:doaj.org-article:6dad3a9b1cfe4e5384f78158ff20c6052021-11-18T06:50:35ZA novel tetrameric PilZ domain structure from xanthomonads.1932-620310.1371/journal.pone.0022036https://doaj.org/article/6dad3a9b1cfe4e5384f78158ff20c6052011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21760949/?tool=EBIhttps://doaj.org/toc/1932-6203PilZ 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 repeat α3 helices to form a parallel four-stranded coiled-coil, which is further enclosed by two sets of inclined α2 and α4 helices. We further generated a series of XCC6012 variants and measured the unfolding temperatures and oligomeric states in order to investigate the nature of this novel tetramer. Discovery of this new PilZ domain architecture increases the complexity of c-di-GMP-mediated regulation.Tso-Ning LiKo-Hsin ChinKit-Man FungMing-Te YangAndrew H-J WangShan-Ho ChouPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 7, p e22036 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tso-Ning Li Ko-Hsin Chin Kit-Man Fung Ming-Te Yang Andrew H-J Wang Shan-Ho Chou A novel tetrameric PilZ domain structure from xanthomonads.
description	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 repeat α3 helices to form a parallel four-stranded coiled-coil, which is further enclosed by two sets of inclined α2 and α4 helices. We further generated a series of XCC6012 variants and measured the unfolding temperatures and oligomeric states in order to investigate the nature of this novel tetramer. Discovery of this new PilZ domain architecture increases the complexity of c-di-GMP-mediated regulation.
format	article
author	Tso-Ning Li Ko-Hsin Chin Kit-Man Fung Ming-Te Yang Andrew H-J Wang Shan-Ho Chou
author_facet	Tso-Ning Li Ko-Hsin Chin Kit-Man Fung Ming-Te Yang Andrew H-J Wang Shan-Ho Chou
author_sort	Tso-Ning Li
title	A novel tetrameric PilZ domain structure from xanthomonads.
title_short	A novel tetrameric PilZ domain structure from xanthomonads.
title_full	A novel tetrameric PilZ domain structure from xanthomonads.
title_fullStr	A novel tetrameric PilZ domain structure from xanthomonads.
title_full_unstemmed	A novel tetrameric PilZ domain structure from xanthomonads.
title_sort	novel tetrameric pilz domain structure from xanthomonads.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/6dad3a9b1cfe4e5384f78158ff20c605
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A novel tetrameric PilZ domain structure from xanthomonads.

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