6cl5

Structure of P. aeruginosa R1 pyocin fiber PALES_06171 comprising C-terminal residues 323-701

spinqualitylabelsall models 6cl5, resolution 2.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cl5 is a 6 chain structure with sequence from Pseudomonas aeruginosa LESB58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.324Å Ligands: FE, MG, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9KW03_PSEAI Publication Abstract from PubMed The R-type pyocins are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. Structurally, the R-type pyocins are similar to "simple" contractile tails, such as those of phage P2 and Mu. The pyocin recognizes and binds to its target with the help of fibers that emanate from the baseplate structure at one end of the particle. Subsequently, the pyocin contracts its sheath and drives the rigid tube through the host cell envelope. This causes depolarization of the cytoplasmic membrane and cell death. The host cell surface-binding fiber is ~340 A-long and is attached to the baseplate with its N-terminal domain. Here, we report the crystal structures of C-terminal fragments of the R1 and R2 pyocin fibers that comprise the distal, receptor-binding part of the protein. Both proteins are ~240 A-long homotrimers in which slender rod-like domains are interspersed with more globular domains-two tandem knob domains in the N-terminal part of the fragment and a lectin-like domain at its C-terminus. The putative substrate binding sites are separated by about 100 A, suggesting that binding of the fiber to the cell surface causes the fiber to adopt a certain orientation relative to the baseplate and this then triggers sheath contraction. Structure and Analysis of R1 and R2 Pyocin Receptor-Binding Fibers.,Buth SA, Shneider MM, Scholl D, Leiman PG Viruses. 2018 Aug 14;10(8). pii: v10080427. doi: 10.3390/v10080427. PMID:30110933 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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