TY - JOUR
T1 - Structure of the cell-puncturing device of bacteriophage T4
AU - Kanamaru, Shuji
AU - Leiman, Petr G.
AU - Kostyuchenko, Victor A.
AU - Chipman, Paul R.
AU - Mesyanzhinov, Vadim V.
AU - Arisaka, Fumio
AU - Rossmann, Michael G.
N1 - Funding Information:
We thank M. Allen for technical help and M. Pique for help with computer graphics. This work was supported by grants from the NIH and by the Skaggs Institute for Chemical Biology. S.J.D. was supported by a fellowship from the NIH.
Funding Information:
We thank T. S. Baker for establishing the electron microscopy facilities at Purdue, where we collected the cryoEM data, A. A. Simpson for advice and help in data collection, and B. W. Matthews for discussion of the results. We thank the staff of BioCARS for their help and advice in the data collection at the Advanced Photon Source beam lines 14-BM-C and 14-BM-D. We thank S. Wilder for help in preparation of the manuscript. The work was supported by a National Science Foundation grant to M.G.R.; Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan to F.A.; a Howard Hughes Medical Institute grant to V.V.M.; a reinvestment grant from Purdue University; and a Keck Foundation award for the purchase of a Philips CM300 electron microscope.
PY - 2002/1/31
Y1 - 2002/1/31
N2 - Bacteriophage T4 has a very efficient mechanism for infecting cells. The key component of this process is the baseplate, located at the end of the phage tail, which regulates the interaction of the tail fibres and the DNA ejection machine. A complex of gene product (gp) 5 (63K) and gp27 (44K), the central part of the baseplate, is required to penetrate the outer cell membrane of Escherichia coli and to disrupt the intermembrane peptidoglycan layer, promoting subsequent entry of phage DNA into the host. We present here a crystal structure of the (gp5-gp27)3 321K complex, determined to 2.9 Å resolution and fitted into a cryo-electron microscopy map at 17 Å resolution of the baseplate-tail tube assembly. The carboxy-terminal domain of gp5 is a triple-stranded β-helix that forms an equilateral triangular prism, which acts as a membrane-puncturing needle. The middle lysozyme domain of gp5, situated on the periphery of the prism, serves to digest the peptidoglycan layer. The amino-terminal, antiparallel β-barrel domain of gp5 is inserted into a cylinder formed by three gp27 monomers, which may serve as a channel for DNA ejection.
AB - Bacteriophage T4 has a very efficient mechanism for infecting cells. The key component of this process is the baseplate, located at the end of the phage tail, which regulates the interaction of the tail fibres and the DNA ejection machine. A complex of gene product (gp) 5 (63K) and gp27 (44K), the central part of the baseplate, is required to penetrate the outer cell membrane of Escherichia coli and to disrupt the intermembrane peptidoglycan layer, promoting subsequent entry of phage DNA into the host. We present here a crystal structure of the (gp5-gp27)3 321K complex, determined to 2.9 Å resolution and fitted into a cryo-electron microscopy map at 17 Å resolution of the baseplate-tail tube assembly. The carboxy-terminal domain of gp5 is a triple-stranded β-helix that forms an equilateral triangular prism, which acts as a membrane-puncturing needle. The middle lysozyme domain of gp5, situated on the periphery of the prism, serves to digest the peptidoglycan layer. The amino-terminal, antiparallel β-barrel domain of gp5 is inserted into a cylinder formed by three gp27 monomers, which may serve as a channel for DNA ejection.
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U2 - 10.1038/415553a
DO - 10.1038/415553a
M3 - Article
C2 - 11823865
AN - SCOPUS:0037203891
SN - 0028-0836
VL - 415
SP - 553
EP - 557
JO - Nature
JF - Nature
IS - 6871
ER -