6hhk

Structure of gp105 of Listeria bacteriophage A511

spinqualitylabelsall models 6hhk, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hhk is a 3 chain structure with sequence from Listeria virus A511. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.38Å Ligands: CL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A8AST9_BPA51 Publication Abstract from PubMed Contractile injection systems (bacteriophage tails, type VI secretions system, R-type pyocins, etc.) utilize a rigid tube/contractile sheath assembly for breaching the envelope of bacterial and eukaryotic cells. Among contractile injection systems, bacteriophages that infect Gram-positive bacteria represent the least understood members. Here, we describe the structure of Listeria bacteriophage A511 tail in its pre- and post-host attachment states (extended and contracted, respectively) using cryo-electron microscopy, cryo-electron tomography, and X-ray crystallography. We show that the structure of the tube-baseplate complex of A511 is similar to that of phage T4, but the A511 baseplate is decorated with different receptor-binding proteins, which undergo a large structural transformation upon host attachment and switch the symmetry of the baseplate-tail fiber assembly from threefold to sixfold. For the first time under native conditions, we show that contraction of the phage tail sheath assembly starts at the baseplate and propagates through the sheath in a domino-like motion. Structure and transformation of bacteriophage A511 baseplate and tail upon infection of Listeria cells.,Guerrero-Ferreira RC, Hupfeld M, Nazarov S, Taylor NM, Shneider MM, Obbineni JM, Loessner MJ, Ishikawa T, Klumpp J, Leiman PG EMBO J. 2019 Feb 1;38(3). pii: embj.201899455. doi: 10.15252/embj.201899455. Epub, 2019 Jan 2. PMID:30606715 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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