6HHK

Structure of gp105 of Listeria bacteriophage A511

Summary for 6HHK

• Entry DOI: 10.2210/pdb6hhk/pdb
• Descriptor: Gp105, CHLORIDE ION (3 entities in total)
• Functional Keywords: bacteriophage baseplate protein, viral protein
• Biological source: Listeria phage A511 (Bacteriophage A511)
• Total number of polymer chains: 3
• Total formula weight: 64480.23

Authors

Taylor, N.M.I.,Guerrero-Ferreira, R.C.,Leiman, P.G. (deposition date: 2018-08-28, release date: 2019-01-23, Last modification date: 2019-02-13)

Primary citation

Guerrero-Ferreira, R.C.,Hupfeld, M.,Nazarov, S.,Taylor, N.M.,Shneider, M.M.,Obbineni, J.M.,Loessner, M.J.,Ishikawa, T.,Klumpp, J.,Leiman, P.G.
Structure and transformation of bacteriophage A511 baseplate and tail upon infection ofListeriacells.
EMBO J., 38:-, 2019

PubMed Abstract: 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 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.

PubMed: 30606715
DOI: 10.15252/embj.201899455

Experimental method

X-RAY DIFFRACTION (2.38 Å)