Structural highlights
Publication Abstract from PubMed
Members of the AAA+ (ATPase associated with various cellular activities) family of ATPases couple chemical energy derived from ATP hydrolysis for generation of mechanical force, resulting in conformational changes. The hydrolysis is brought about by highly conserved domains and motifs. The sensor I motif is critical for sensing and hydrolysis of the nucleotide. Pseudomonas aeruginosa FleQ is an ATPase that is a positive regulator of flagellar gene expression. We have determined the crystal structures of the ATPase domain of wild-type FleQ and sensor I mutants H287N and H287A in complex with ATPgammaS and Mg(2+) to 2.4, 1.95, and 2.25 A resolution, respectively. The structural data highlight the role of sensor I in regulating the ATPase activity. The in vitro and in vivo data demonstrate that the moderate ATPase activity of FleQ due to the presence of histidine in sensor I is essential for maintaining the monotrichous phenotype and for the rapid motility to biofilm transition.
Sensor I Regulated ATPase Activity of FleQ Is Essential for Motility to Biofilm Transition in Pseudomonas aeruginosa.,Banerjee P, Chanchal, Jain D ACS Chem Biol. 2019 Jul 19;14(7):1515-1527. doi: 10.1021/acschembio.9b00255. Epub, 2019 Jul 3. PMID:31268665[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Banerjee P, Chanchal, Jain D. Sensor I Regulated ATPase Activity of FleQ Is Essential for Motility to Biofilm Transition in Pseudomonas aeruginosa. ACS Chem Biol. 2019 Jul 19;14(7):1515-1527. doi: 10.1021/acschembio.9b00255. Epub, 2019 Jul 3. PMID:31268665 doi:http://dx.doi.org/10.1021/acschembio.9b00255
