5J1J

Structure of FleN-AMPPNP complex

Summary for 5J1J

• Entry DOI: 10.2210/pdb5j1j/pdb
• Descriptor: Site-determining protein, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, SULFATE ION, ... (5 entities in total)
• Functional Keywords: flen, transcription, antiactivator, amppnp
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 2
• Total formula weight: 62509.94

Authors

Jain, D.,Chanchal,Banerjee, P. (deposition date: 2016-03-29, release date: 2017-03-29, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.55 Å)