3AJW

Structure of FliJ, a soluble component of flagellar type III export apparatus

3AJW の概要

• エントリーDOI: 10.2210/pdb3ajw/pdb
• 分子名称: Flagellar fliJ protein, MERCURY (II) ION (3 entities in total)
• 機能のキーワード: flagellum, type iii secretion, coiled-coil, protein transport
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P0A1K1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17829.53

構造登録者

Imada, K.,Ibuki, T.,Minamino, T.,Namba, K. (登録日: 2010-06-23, 公開日: 2011-02-02, 最終更新日: 2024-03-13)

主引用文献

Ibuki, T.,Imada, K.,Minamino, T.,Kato, T.,Miyata, T.,Namba, K.
Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases
Nat.Struct.Mol.Biol., 18:277-282, 2011

PubMed Abstract: The proteins that form the bacterial flagellum are translocated to its distal end through the central channel of the growing flagellum by the flagellar-specific protein export apparatus, a family of the type III protein secretion system. FliI and FliJ are soluble components of this apparatus. FliI is an ATPase that has extensive structural similarity to the α and β subunits of F(o)F(1)-ATP synthase. FliJ is essential for export, but its function remains obscure. Here we show that the structure of FliJ derived from Salmonella enterica serovar Typhimurium is remarkably similar to that of the two-stranded α-helical coiled-coil part of the γ subunit of F(o)F(1)-ATP synthase and that FliJ promotes the formation of FliI hexamer rings by binding to the center of the ring. These results suggest that the type III protein export system and F- and V-type ATPases share a similar mechanism and an evolutionary relationship.

PubMed: 21278755
DOI: 10.1038/nsmb.1977

実験手法

X-RAY DIFFRACTION (2.1 Å)