2vnl

MUTANT Y108Wdel OF THE HEADBINDING DOMAIN OF PHAGE P22 TAILSPIKE C- TERMINally fused to ISOLEUCINE ZIPPER pIIGCN4 (chimera II)

spinqualitylabelsall models 2vnl, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vnl is a 1 chain structure with sequence from Bpp22. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Related: 2vfo, 2vky, 2vfn, 2vfq, 1qrc, 1clw, 1qrb, 1tsp, 1qa2, 2vfp, 2vfm, 1lkt, 1qa3, 1tyv, 1qa1, 1qq1, 2xc1 Resources: FirstGlance, OCA, RCSB, PDBsum Function [TSPE_BPP22] Non-covalently bound to the neck of the phage capsid and mediating attachment of the viral particle to host cell-surface polysaccharide. It displays endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Attachment of phages to host cells, followed by phage DNA ejection, represents the first stage of viral infection of bacteria. Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral tailspike protein for attachment. While the structures of the N-terminal particle-binding domain and the major receptor-binding domain of the tailspike have been analyzed individually, the three-dimensional organization of the intact protein, including the highly conserved linker region between the two domains, remained unknown. A single amino-acid exchange in the linker sequence made it possible to crystallize the full-length protein. Two crystal structures of the linker region are presented: one attached to the N-terminal domain and the other present within the complete tailspike protein. Both retain their biological function, but the mutated full-length tailspike displays a retarded folding pathway. Fitting of the full-length tailspike into a published cryo-electron microscopy map of the P22 virion requires an elastic distortion of the crystal structure. The conservation of the linker suggests a role in signal transmission from the distal tip of the molecule to the phage head, eventually leading to DNA ejection. Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker.,Seul A, Muller JJ, Andres D, Stettner E, Heinemann U, Seckler R Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1336-45. doi:, 10.1107/S1399004714002685. Epub 2014 Apr 30. PMID:24816102 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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