6J7E
Crystal Structure of Central domain of FleQ in complex with ATPgS and Mg
Summary for 6J7E
| Entry DOI | 10.2210/pdb6j7e/pdb |
| Descriptor | Nitrogen assimilation regulatory protein, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | fleq, pseudomonas, aaa+, ntrc, transcription |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 30239.58 |
| Authors | Banerjee, P.,Chanchal,Jain, D. (deposition date: 2019-01-18, release date: 2019-11-27, Last modification date: 2023-11-22) |
| Primary citation | Banerjee, P.,Chanchal,Jain, D. Sensor I Regulated ATPase Activity of FleQ Is Essential for Motility to Biofilm Transition inPseudomonas aeruginosa. Acs Chem.Biol., 14:1515-1527, 2019 Cited by PubMed Abstract: 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. 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 ATPγS and Mg to 2.4, 1.95, and 2.25 Å resolution, respectively. The structural data highlight the role of sensor I in regulating the ATPase activity. The and 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. PubMed: 31268665DOI: 10.1021/acschembio.9b00255 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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