TY - JOUR
T1 - The tail structure of bacteriophage T4 and its mechanism of contraction
AU - Kostyuchenko, Victor A.
AU - Chipman, Paul R.
AU - Leiman, Petr G.
AU - Arisaka, Fumio
AU - Mesyanzhinov, Vadim V.
AU - Rossmann, Michael G.
N1 - Funding Information:
We thank S. Wilder and C. Towell for help in the preparation of the manuscript. The work was supported by a US National Science Foundation grant to M.G.R., a Howard Hughes Medical Institute grant and a Russian Fund for Basic Research grant to V.V.M., a Human Frontiers Science Program grant to M.G.R., F.A. and V.V.M., a Keck Foundation grant to M.G.R. for the purchase of the Philips CM300 field emission gun microscope and a reinvestment grant from Purdue University.
Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/9
Y1 - 2005/9
N2 - Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail assembly at 15-Å resolution shows the hexagonal dome-shaped baseplate, the extended contractile sheath, the long tail fibers attached to the baseplate and the collar formed by six whiskers that interact with the long tail fibers. Comparison with the structure of the contracted tail shows that tail contraction is associated with a substantial rearrangement of the domains within the sheath protein and results in shortening of the sheath to about one-third of its original length. During contraction, the tail tube extends beneath the baseplate by about one-half of its total length and rotates by 345°, allowing it to cross the host's periplasmic space.
AB - Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail assembly at 15-Å resolution shows the hexagonal dome-shaped baseplate, the extended contractile sheath, the long tail fibers attached to the baseplate and the collar formed by six whiskers that interact with the long tail fibers. Comparison with the structure of the contracted tail shows that tail contraction is associated with a substantial rearrangement of the domains within the sheath protein and results in shortening of the sheath to about one-third of its original length. During contraction, the tail tube extends beneath the baseplate by about one-half of its total length and rotates by 345°, allowing it to cross the host's periplasmic space.
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U2 - 10.1038/nsmb975
DO - 10.1038/nsmb975
M3 - Article
C2 - 16116440
AN - SCOPUS:26944500906
SN - 1545-9993
VL - 12
SP - 810
EP - 813
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
IS - 9
ER -