8RKL

TadA/CpaF nucleotide free

8RKL の概要

• エントリーDOI: 10.2210/pdb8rkl/pdb
• EMDBエントリー: 19279
• 分子名称: Pilus assembly ATPase CpaF, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (2 entities in total)
• 機能のキーワード: secretion, atpase, apo, motor protein
• 由来する生物種: Caulobacter vibrioides NA1000
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 279744.41

構造登録者

Hohl, M.,Low, H. (登録日: 2023-12-26, 公開日: 2024-08-14)

主引用文献

Hohl, M.,Banks, E.J.,Manley, M.P.,Le, T.B.K.,Low, H.H.
Bidirectional pilus processing in the Tad pilus system motor CpaF.
Nat Commun, 15:6635-6635, 2024

PubMed Abstract: The bacterial tight adherence pilus system (TadPS) assembles surface pili essential for adhesion and colonisation in many human pathogens. Pilus dynamics are powered by the ATPase CpaF (TadA), which drives extension and retraction cycles in Caulobacter crescentus through an unknown mechanism. Here we use cryogenic electron microscopy and cell-based light microscopy to characterise CpaF mechanism. We show that CpaF assembles into a hexamer with C2 symmetry in different nucleotide states. Nucleotide cycling occurs through an intra-subunit clamp-like mechanism that promotes sequential conformational changes between subunits. Moreover, a comparison of the active sites with different nucleotides bound suggests a mechanism for bidirectional motion. Conserved CpaF residues, predicted to interact with platform proteins CpaG (TadB) and CpaH (TadC), are mutated in vivo to establish their role in pilus processing. Our findings provide a model for how CpaF drives TadPS pilus dynamics and have broad implications for how other ancient type 4 filament family members power pilus assembly.

PubMed: 39103374
DOI: 10.1038/s41467-024-50280-6

実験手法

ELECTRON MICROSCOPY (4 Å)