3RQA

The Crystal Structure of a Pathogenic Protein from the Xanthomonas campestris Reveals a New Tetrameric PilZ Domain Self-Assembled via a Unusual Helical Bundle

3RQA の概要

• エントリーDOI: 10.2210/pdb3rqa/pdb
• 分子名称: Putative uncharacterized protein, ACETATE ION (3 entities in total)
• 機能のキーワード: pilz domain, tetrameric parallel coiled-coil, four helix bundle, unknown function
• 由来する生物種: Xanthomonas campestris pv. campestris
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 84203.37

構造登録者

Li, T.-N.,Chin, K.-H.,Chou, S.-H. (登録日: 2011-04-28, 公開日: 2012-03-14, 最終更新日: 2024-03-20)

主引用文献

Li, T.-N.,Chin, K.-H.,Fung, K.-M.,Yang, M.-T.,Wang, A.H.-J.,Chou, S.-H.
A novel tetrameric PilZ domain structure from xanthomonads
Plos One, 6:e22036-e22036, 2011

PubMed 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 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.

PubMed: 21760949
DOI: 10.1371/journal.pone.0022036

実験手法

X-RAY DIFFRACTION (2.1 Å)