Three-dimensional structure of the bacteriophage P22 tail machine

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 reconstructio...

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Detalles Bibliográficos
Autores principales: Tang, Liang, Marion, William R, Cingolani, Gino, Prevelige, Peter E, Johnson, John E
Formato: Texto
Lenguaje:English
Publicado: 2005
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1150889/
https://www.ncbi.nlm.nih.gov/pubmed/15933718
http://dx.doi.org/10.1038/sj.emboj.7600695
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author Tang, Liang
Marion, William R
Cingolani, Gino
Prevelige, Peter E
Johnson, John E
author_facet Tang, Liang
Marion, William R
Cingolani, Gino
Prevelige, Peter E
Johnson, John E
author_sort Tang, Liang
collection PubMed
description 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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spelling pubmed-11508892005-06-15 Three-dimensional structure of the bacteriophage P22 tail machine Tang, Liang Marion, William R Cingolani, Gino Prevelige, Peter E Johnson, John E EMBO J Article 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. 2005-06-15 2005-06-02 /pmc/articles/PMC1150889/ /pubmed/15933718 http://dx.doi.org/10.1038/sj.emboj.7600695 Text en Copyright © 2005, European Molecular Biology Organization
spellingShingle Article
Tang, Liang
Marion, William R
Cingolani, Gino
Prevelige, Peter E
Johnson, John E
Three-dimensional structure of the bacteriophage P22 tail machine
title Three-dimensional structure of the bacteriophage P22 tail machine
title_full Three-dimensional structure of the bacteriophage P22 tail machine
title_fullStr Three-dimensional structure of the bacteriophage P22 tail machine
title_full_unstemmed Three-dimensional structure of the bacteriophage P22 tail machine
title_short Three-dimensional structure of the bacteriophage P22 tail machine
title_sort three-dimensional structure of the bacteriophage p22 tail machine
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1150889/
https://www.ncbi.nlm.nih.gov/pubmed/15933718
http://dx.doi.org/10.1038/sj.emboj.7600695
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AT cingolanigino threedimensionalstructureofthebacteriophagep22tailmachine
AT preveligepetere threedimensionalstructureofthebacteriophagep22tailmachine
AT johnsonjohne threedimensionalstructureofthebacteriophagep22tailmachine

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