6JDL

Central domain of FleQ H287A mutant in complex with ATPgS and Mg

6JDL の概要

• エントリーDOI: 10.2210/pdb6jdl/pdb
• 分子名称: Nitrogen assimilation regulatory protein, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: fleq, pseudomonas, aaa+, ntrc, transcription
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30080.42

構造登録者

Jain, D.,Banerjee, P.,Chanchal (登録日: 2019-02-01, 公開日: 2019-11-27, 最終更新日: 2023-11-22)

主引用文献

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

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: 31268665
DOI: 10.1021/acschembio.9b00255

実験手法

X-RAY DIFFRACTION (2.249 Å)