4zhw

Crystal structure of a bacterial signalling protein (N-terminal truncation)

spinqualitylabelsall models 4zhw, resolution 1.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zhw is a 1 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 1.391Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9I4L6_PSEAE Publication Abstract from PubMed YfiBNR is a tripartite signalling system in Pseudomonas aeruginosa that modulates intracellular c-di-GMP levels in response to signals received in the periplasm. YfiB is an outer membrane lipoprotein and presumed sensor protein that sequesters the repressor protein YfiR. To provide insights into YfiBNR function, we have determined three-dimensional crystal structures of YfiB and YfiR from P. aeruginosa PAO1 alone and as a 1:1 complex. A YfiB(27-168) construct is predominantly dimeric, whereas a YfiB(59-168) is monomeric, indicating that YfiB can dimerize via its N-terminal region. YfiR forms a stable complex with YfiB(59-168), while the YfiR binding interface is obstructed by the N-terminal region in YfiB(27-168). The YfiB-YfiR complex reveals a conserved interaction surface on YfiR that overlaps with residues predicted to interact with the periplasmic PAS domain of YfiN. Comparison of native and YfiR-bound structures of YfiB suggests unwinding of the N-terminal linker region for attachment to the outer membrane. A model is thus proposed for YfiR sequestration at the outer membrane by YfiB. Our work provides the first detailed insights into the interaction between YfiB and YfiR at the molecular level and is a valuable starting point for further functional and mechanistic studies of the YfiBNR signalling system. Structural insights into YfiR sequestering by YfiB in Pseudomonas aeruginosa PAO1.,Li S, Li T, Xu Y, Zhang Q, Zhang W, Che S, Liu R, Wang Y, Bartlam M Sci Rep. 2015 Nov 23;5:16915. doi: 10.1038/srep16915. PMID:26593397 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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