4wxm | pdb_00004wxm

FleQ REC domain from Pseudomonas aeruginosa PAO1

spinqualitylabelsall models 4wxm, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wxm is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4wxo Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed 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 2.3A 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. The REC domain mediated dimerization is critical for FleQ from Pseudomonas aeruginosa to function as a c-di-GMP receptor and flagella gene regulator.,Su T, Liu S, Wang K, Chi K, Zhu D, Wei T, Huang Y, Guo L, Hu W, Xu S, Lin Z, Gu L J Struct Biol. 2015 Oct;192(1):1-13. doi: 10.1016/j.jsb.2015.09.002. Epub 2015, Sep 8. PMID:26362077 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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