5OIU

Crystal structure of PilF type IV pilus assembly ATPase from Thermus thermophilus

5OIU の概要

• エントリーDOI: 10.2210/pdb5oiu/pdb
• 分子名称: Type IV pilus assembly protein PilF, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: atpase, aaa+, type iv pilus, dna binding protein, atp, motor protein
• 由来する生物種: Thermus thermophilus HB8
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 262766.53

構造登録者

Karuppiah, V.,Derrick, J.P. (登録日: 2017-07-19, 公開日: 2018-08-08, 最終更新日: 2024-01-17)

主引用文献

Collins, R.,Karuppiah, V.,Siebert, C.A.,Dajani, R.,Thistlethwaite, A.,Derrick, J.P.
Structural cycle of the Thermus thermophilus PilF ATPase: the powering of type IVa pilus assembly.
Sci Rep, 8:14022-14022, 2018

PubMed Abstract: Type IV pili are responsible for a diverse range of functions, including twitching motility and cell adhesion. Assembly of the pilus fiber is driven by a cytoplasmic ATPase: it interacts with an inner membrane complex of biogenesis proteins which, in turn, bind to nascent pilin subunits and mediate fiber assembly. Here we report the structural characterization of the PilF TFP assembly ATPase from Thermus thermophilus. The crystal structure of a recombinant C-terminal fragment of PilF revealed bound, unhydrolysed ATP, although the full length complex was enzymatically active. 3D reconstructions were carried out by single particle cryoelectron microscopy for full length apoprotein PilF and in complex with AMPPNP. The structure forms an hourglass-like shape, with the ATPase domains in one half and the N1 domains in the second half which, we propose, interact with the other pilus biogenesis components. Molecular models for both forms were generated: binding of AMPPNP causes an upward shift of the N1 domains towards the ATPase domains of ~8 Å. We advocate a model in which ATP hydrolysis is linked to displacement of the N1 domains which is associated with lifting pilin subunits out of the inner membrane, and provide the activation energy needed to form the pilus fiber.

PubMed: 30232337
DOI: 10.1038/s41598-018-32218-3

実験手法

X-RAY DIFFRACTION (2.44 Å)