6ikk
From Proteopedia
Crystal structure of YfiB(L43P) in complex with YfiR
Structural highlights
FunctionYFIB_PSEAE Activates the diguanylate cyclase TpbB/YfiN by sequestering YfiR at the outer membrane, which counteracts the YfiR-mediated repression of TpbB/YfiN at the inner membrane and leads to increased c-di-GMP production (PubMed:20300602, PubMed:22719254). May act as a sensor of envelope stress (PubMed:20300602, PubMed:22719254).[1] [2] Part of the YfiB-TpbB-YfiR (or yfiBNR) system, encoding a tripartite signaling module that modulates intracellular c-di-GMP levels (PubMed:20300602, PubMed:22719254). The system is a key regulator of the small colony variant (SCV) phenotype, and plays an important role in biofilm formation and in vivo persistence (PubMed:20300602). The c-di-GMP produced by TpbB/YfiN stimulates the production of the Pel and Psl exopolysaccharides, which promotes surface attachment, generates an SCV phenotype and confers resistance against phagocytosis (PubMed:20300602).[3] [4] Publication Abstract from PubMedBacterial cyclic-di-GMP (c-di-GMP) is an important messenger molecule that influences diverse cellular processes including motility, virulence and cytotoxicity systems, polysaccharide synthesis and biofilm formation. The YfiBNR tripartite signalling system in P. aeruginosa modulates the cellular c-di-GMP levels in response to signals received from the periplasm. In this study, we analyse the structures of activating mutants of the outer membrane protein YfiB that give rise to increased surface attachment and biofilm formation. The F48S and W55L mutants of YfiB(27-168) crystallize in the same dimeric arrangement as our previously reported YfiB structures that preclude complex formation with YfiR. The L43P mutant of YfiB(27-168) is monomeric and forms a stable complex with YfiR. The YfiB(L43P)-YfiR crystal structure reveals a dramatic rearrangement of the N-terminal fragment, which is implicated in increased YfiB activation and membrane attachment, upon YfiR binding. Comparison with our previous complex structure between YfiB(59-168) and YfiR reveals extensive interactions between the N-terminal fragment of YfiB (residues 35-55) and YfiR. Structural analysis of activating mutants of YfiB from Pseudomonas aeruginosa PAO1.,Li S, Li T, Teng X, Lou X, Xu Y, Zhang Q, Bartlam M Biochem Biophys Res Commun. 2018 Dec 2;506(4):997-1003. doi:, 10.1016/j.bbrc.2018.10.190. Epub 2018 Nov 4. PMID:30404734[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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