5JVF

Crystal Structure of Apo-FleN

5JVF の概要

• エントリーDOI: 10.2210/pdb5jvf/pdb
• 分子名称: Site-determining protein, IODIDE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: flen, transcription, antiactivator, pseudomonas
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32502.44

構造登録者

Jain, D.,Chanchal,Banerjee, P. (登録日: 2016-05-11, 公開日: 2017-03-29, 最終更新日: 2024-03-20)

主引用文献

Chanchal,Banerjee, P.,Jain, D.
ATP-Induced Structural Remodeling in the Antiactivator FleN Enables Formation of the Functional Dimeric Form
Structure, 25:243-252, 2017

PubMed Abstract: FleN, a P loop ATPase is vital for maintaining a monotrichous phenotype in Pseudomonas aeruginosa. FleN exhibits antagonistic activity against FleQ, the master transcriptional regulator of flagellar genes. Crystal structures of FleN in the apo form (1.66 Å) and in complex with β,γ-imidoadenosine 5'-triphosphate (1.55 Å) reveal that it undergoes drastic conformational changes on ATP binding to attain a structure capable of dimerization. Mutations of the residues that stabilize the binding of ATP were defective in their ability to dimerize and do not inhibit ATP hydrolysis by FleQ. Conversely, the catalytic mutant of FleN, was an efficient inhibitor. These observations posit that the dimer is the functional form of FleN and it is nucleotide binding and not hydrolysis by FleN that is necessary to exert an antagonistic effect against FleQ. Our study shows that ATP-induced dimerization may be a strategy to achieve reversible inhibition of FleQ to fine-tune the function of this activator to an optimal level.

PubMed: 28065505
DOI: 10.1016/j.str.2016.11.022

実験手法

X-RAY DIFFRACTION (1.66 Å)