5wk5 | pdb_00005wk5

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Cryo-EM structure of P. aeruginosa flagellar filaments A443V

spinqualitylabelsall models 5wk5, resolution 4.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wk5 is a 41 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: fliC, PA1092 (PSEAE) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Function [FLICB_PSEAE] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Publication Abstract from PubMed The bacterial flagellar filament has long been studied to understand how a polymer composed of a single protein can switch between different supercoiled states with high cooperativity. Here we present near-atomic resolution cryo-EM structures for flagellar filaments from both Gram-positive Bacillus subtilis and Gram-negative Pseudomonas aeruginosa. Seven mutant flagellar filaments in B. subtilis and two in P. aeruginosa capture two different states of the filament. These reliable atomic models of both states reveal conserved molecular interactions in the interior of the filament among B. subtilis, P. aeruginosa and Salmonella enterica. Using the detailed information about the molecular interactions in two filament states, we successfully predict point mutations that shift the equilibrium between those two states. Further, we observe the dimerization of P. aeruginosa outer domains without any perturbation of the conserved interior of the filament. Our results give new insights into how the flagellin sequence has been "tuned" over evolution.Bacterial flagellar filaments are composed almost entirely of a single protein-flagellin-which can switch between different supercoiled states in a highly cooperative manner. Here the authors present near-atomic resolution cryo-EM structures of nine flagellar filaments, and begin to shed light on the molecular basis of filament switching. A structural model of flagellar filament switching across multiple bacterial species.,Wang F, Burrage AM, Postel S, Clark RE, Orlova A, Sundberg EJ, Kearns DB, Egelman EH Nat Commun. 2017 Oct 16;8(1):960. doi: 10.1038/s41467-017-01075-5. PMID:29038601 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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