Three-dimensional structure of the bacteriophage P22 tail machine |
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Authors: | Tang Liang Marion William R Cingolani Gino Prevelige Peter E Johnson John E |
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Affiliation: | Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. |
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Abstract: | The tail of the bacteriophage P22 is composed of multiple protein components and integrates various biological functions that are crucial to the assembly and infection of the phage. The three-dimensional structure of the P22 tail machine determined by electron cryo-microscopy and image reconstruction reveals how the five types of polypeptides present as 51 subunits are organized into this molecular machine through twelve-, six- and three-fold symmetry, and provides insights into molecular events during host cell attachment and phage DNA translocation. |
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Keywords: | bacteriophage electron cryo-microscopy molecular machine symmetry tail |
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