6ikk | pdb_00006ikk

Crystal structure of YfiB(L43P) in complex with YfiR

spinqualitylabelsall models 6ikk, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ikk is a 4 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.19Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9I4L6_PSEAE Publication Abstract from PubMed Bacterial 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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