4IHQ

Archaellum Assembly ATPase FlaI bound to ADP

4IHQ の概要

• エントリーDOI: 10.2210/pdb4ihq/pdb
• 関連するPDBエントリー: 4II7
• 分子名称: FlaI ATPase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: hexamer, hydrolase, atp/adp, membrane associated
• 由来する生物種: Sulfolobus acidocaldarius
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 177967.87

構造登録者

Reindl, S.,Williams, G.J.,Tainer, J.A. (登録日: 2012-12-19, 公開日: 2013-03-06, 最終更新日: 2024-02-28)

主引用文献

Reindl, S.,Ghosh, A.,Williams, G.J.,Lassak, K.,Neiner, T.,Henche, A.L.,Albers, S.V.,Tainer, J.A.
Insights into FlaI Functions in Archaeal Motor Assembly and Motility from Structures, Conformations, and Genetics.
Mol.Cell, 49:1069-1082, 2013

PubMed Abstract: Superfamily ATPases in type IV pili, type 2 secretion, and archaella (formerly archaeal flagella) employ similar sequences for distinct biological processes. Here, we structurally and functionally characterize prototypical superfamily ATPase FlaI in Sulfolobus acidocaldarius, showing FlaI activities in archaeal swimming-organelle assembly and movement. X-ray scattering data of FlaI in solution and crystal structures with and without nucleotide reveal a hexameric crown assembly with key cross-subunit interactions. Rigid building blocks form between N-terminal domains (points) and neighboring subunit C-terminal domains (crown ring). Upon nucleotide binding, these six cross-subunit blocks move with respect to each other and distinctly from secretion and pilus ATPases. Crown interactions and conformations regulate assembly, motility, and force direction via a basic-clamp switching mechanism driving conformational changes between stable, backbone-interconnected moving blocks. Collective structural and mutational results identify in vivo functional components for assembly and motility, phosphate-triggered rearrangements by ATP hydrolysis, and molecular predictors for distinct ATPase superfamily functions.

PubMed: 23416110
DOI: 10.1016/j.molcel.2013.01.014

実験手法

X-RAY DIFFRACTION (2 Å)