4WXM

FleQ REC domain from Pseudomonas aeruginosa PAO1

Summary for 4WXM

• Entry DOI: 10.2210/pdb4wxm/pdb
• Related: 4WXO
• Descriptor: Transcriptional regulator FleQ (2 entities in total)
• Functional Keywords: ntrc superfamily, regulatory domain, c-di-gmp binding, biofilm, transcription regulator
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 5
• Total formula weight: 81366.93

Authors

Su, T.,Liu, S.,Gu, L. (deposition date: 2014-11-14, release date: 2015-09-23, Last modification date: 2024-03-20)

Primary citation

Su, T.,Liu, S.,Wang, K.,Chi, K.,Zhu, D.,Wei, T.,Huang, Y.,Guo, L.,Hu, W.,Xu, S.,Lin, Z.,Gu, L.
The REC domain mediated dimerization is critical for FleQ from Pseudomonas aeruginosa to function as a c-di-GMP receptor and flagella gene regulator
J.Struct.Biol., 192:1-13, 2015

PubMed Abstract: FleQ is an AAA+ ATPase enhancer-binding protein that regulates both flagella and biofilm formation in the opportunistic pathogen Pseudomonas aeruginosa. FleQ belongs to the NtrC subfamily of response regulators, but lacks the corresponding aspartic acid for phosphorylation in the REC domain (FleQ(R), also named FleQ domain). Here, we show that the atypical REC domain of FleQ is essential for the function of FleQ. Crystal structure of FleQ(R) at 2.3Å reveals that the structure of FleQ(R) is significantly different from the REC domain of NtrC1 which regulates gene expression in a phosphorylation dependent manner. FleQ(R) forms a novel active dimer (transverse dimer), and mediates the dimerization of full-length FleQ in an unusual manner. Point mutations that affect the dimerization of FleQ lead to loss of function of the protein. Moreover, a c-di-GMP binding site deviating from the previous reported one is identified through structure analysis and point mutations.

PubMed: 26362077
DOI: 10.1016/j.jsb.2015.09.002

Experimental method

X-RAY DIFFRACTION (2.3 Å)