TY - JOUR
T1 - Phage pierces the host cell membrane with the iron-loaded spike
AU - Browning, Christopher
AU - Shneider, Mikhail M.
AU - Bowman, Valorie D.
AU - Schwarzer, David
AU - Leiman, Petr G.
N1 - Funding Information:
Phage P2 DNA was kindly provided by Prof. Haggård-Ljungquist (Stockholm University). We express our sincere thanks to the entire staff of the protein crystallography beam lines at the Swiss Light Source and, in particular, to Dr. Meitian Wang, Dr. Takashi Tomizaki, Dr. Vincent Olieric, Dr. Martin Fuchs, Dr. Florian Dworkowski, and Dr. Clemens Schulze-Briese. We are very grateful to Victor Kostyuchenko, who wrote a script for identification of all protein sequences containing the HxH motif in the T4 genome. We thank Jozef Adamcik for AFM imaging of ϕ92. This work was supported by EPFL, the Swiss National Science Foundation (Grant 31003A-127092/1), and the Scientific and Technological Cooperation Programme Switzerland-Russia. D.S. was supported in part by the Deutsche Forschungsgemeinschaft (DFG) in the framework of DFG Research Unit 548 (Grants Ge801/7-1 and 7-2).
PY - 2012/2/8
Y1 - 2012/2/8
N2 - Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long β-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and 92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a ∼10 diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding.
AB - Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long β-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and 92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a ∼10 diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding.
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U2 - 10.1016/j.str.2011.12.009
DO - 10.1016/j.str.2011.12.009
M3 - Article
C2 - 22325780
AN - SCOPUS:84856753664
SN - 0969-2126
VL - 20
SP - 326
EP - 339
JO - Structure
JF - Structure
IS - 2
ER -