2DPY

Crystal structure of the flagellar type III ATPase FliI

2DPY の概要

• エントリーDOI: 10.2210/pdb2dpy/pdb
• 分子名称: Flagellum-specific ATP synthase, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: beta barrel, alpha-beta structure, hydrolase
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cytoplasm (Potential): P26465
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94761.31

構造登録者

Imada, K.,Namba, K.,Minamino, T. (登録日: 2006-05-18, 公開日: 2006-12-26, 最終更新日: 2024-03-13)

主引用文献

Imada, K.,Minamino, T.,Tahara, A.,Namba, K.
Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits
Proc.Natl.Acad.Sci.Usa, 104:485-490, 2007

PubMed Abstract: Construction of the bacterial flagellum in the cell exterior proceeds at its distal end by highly ordered self-assembly of many different component proteins, which are selectively exported through the central channel of the growing flagellum by the flagellar type III export apparatus. FliI is the ATPase of the export apparatus that drives the export process. Here we report the 2.4 A resolution crystal structure of FliI in the ADP-bound form. FliI consists of three domains, and the whole structure shows extensive similarities to the alpha and beta subunits of F0F1-ATPsynthase, a rotary motor that drives the chemical reaction of ATP synthesis. A hexamer model of FliI has been constructed based on the F1-ATPase structure composed of the alpha3beta3gamma subunits. Although the regions that differ in conformation between FliI and the F1-alpha/beta subunits are all located on the outer surface of the hexamer ring, the main chain structures at the subunit interface and those surrounding the central channel of the ring are well conserved. These results imply an evolutionary relation between the flagellum and F0F1-ATPsynthase and a similarity in the mechanism between FliI and F1-ATPase despite the apparently different functions of these proteins.

PubMed: 17202259
DOI: 10.1073/pnas.0608090104

実験手法

X-RAY DIFFRACTION (2.4 Å)