6KTY

Crystal structure of the flagellar cap protein FliD from Bdellovibrio bacteriovorus

6KTY の概要

• エントリーDOI: 10.2210/pdb6kty/pdb
• 分子名称: Flagellar hook-associated protein 2 (2 entities in total)
• 機能のキーワード: bacterial flagellar cap protein, structural protein
• 由来する生物種: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21218.66

構造登録者

Cho, S.Y.,Yoon, S.I. (登録日: 2019-08-29, 公開日: 2019-10-09, 最終更新日: 2024-03-27)

主引用文献

Cho, S.Y.,Song, W.S.,Yoon, S.I.
Crystal structure of the flagellar cap protein FliD from Bdellovibrio bacteriovorus.
Biochem.Biophys.Res.Commun., 519:652-658, 2019

PubMed Abstract: Bdellovibrio bacteriovorus is a predator bacterial species of the Deltaproteobacteria class that requires flagellum-mediated motility to initiate the parasitization of other gram-negative bacteria. The flagellum is capped by FliD, which polymerizes flagellin into a flagellar filament. FliD has been reported to function as a species-specific oligomer, such as a tetramer, a pentamer, or a hexamer, in members of the Gammaproteobacteria class. However, the oligomeric state and structural features of FliD from bacterial species outside the Gammaproteobacteria class are unknown. Based on structural and biochemical analyses, we report here that B. bacteriovorus FliD (bbFliD) forms a tetramer. bbFliD tetramerizes in a circular head-to-tail arrangement by inserting the D2 domain of one subunit into the concave surface of the second subunit generated between the D2 and D3 domains as observed in Serratia marcescens FliD. However, bbFliD adopts a more compact and flat oligomeric structure, which exhibits a more extended tetramerization interface flanked by two additional surfaces due to different intersubunit and interdomain organizations as well as an elongated loop. In conclusion, FliD from B. bacteriovorus, which belongs to the Deltaproteobacteria class, also produces a tetramer similar to FliD from Gammaproteobacterial species but adopts a unique species-specific oligomeric structure.

PubMed: 31542231
DOI: 10.1016/j.bbrc.2019.09.024

実験手法

X-RAY DIFFRACTION (1.99 Å)