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Morphogenesis of the T4 tail and tail fibers
Remarkable progress has been made during the past ten years in elucidating the structure of the bacteriophage T4 tail by a combination of three-dimensional image reconstruction from electron micrographs and X-ray crystallography of the components. Partial and complete structures of nine out of twent...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3004832/ https://www.ncbi.nlm.nih.gov/pubmed/21129200 http://dx.doi.org/10.1186/1743-422X-7-355 |
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author | Leiman, Petr G Arisaka, Fumio van Raaij, Mark J Kostyuchenko, Victor A Aksyuk, Anastasia A Kanamaru, Shuji Rossmann, Michael G |
author_facet | Leiman, Petr G Arisaka, Fumio van Raaij, Mark J Kostyuchenko, Victor A Aksyuk, Anastasia A Kanamaru, Shuji Rossmann, Michael G |
author_sort | Leiman, Petr G |
collection | PubMed |
description | Remarkable progress has been made during the past ten years in elucidating the structure of the bacteriophage T4 tail by a combination of three-dimensional image reconstruction from electron micrographs and X-ray crystallography of the components. Partial and complete structures of nine out of twenty tail structural proteins have been determined by X-ray crystallography and have been fitted into the 3D-reconstituted structure of the "extended" tail. The 3D structure of the "contracted" tail was also determined and interpreted in terms of component proteins. Given the pseudo-atomic tail structures both before and after contraction, it is now possible to understand the gross conformational change of the baseplate in terms of the change in the relative positions of the subunit proteins. These studies have explained how the conformational change of the baseplate and contraction of the tail are related to the tail's host cell recognition and membrane penetration function. On the other hand, the baseplate assembly process has been recently reexamined in detail in a precise system involving recombinant proteins (unlike the earlier studies with phage mutants). These experiments showed that the sequential association of the subunits of the baseplate wedge is based on the induced-fit upon association of each subunit. It was also found that, upon association of gp53 (gene product 53), the penultimate subunit of the wedge, six of the wedge intermediates spontaneously associate to form a baseplate-like structure in the absence of the central hub. Structure determination of the rest of the subunits and intermediate complexes and the assembly of the hub still require further study. |
format | Text |
id | pubmed-3004832 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-30048322010-12-21 Morphogenesis of the T4 tail and tail fibers Leiman, Petr G Arisaka, Fumio van Raaij, Mark J Kostyuchenko, Victor A Aksyuk, Anastasia A Kanamaru, Shuji Rossmann, Michael G Virol J Review Remarkable progress has been made during the past ten years in elucidating the structure of the bacteriophage T4 tail by a combination of three-dimensional image reconstruction from electron micrographs and X-ray crystallography of the components. Partial and complete structures of nine out of twenty tail structural proteins have been determined by X-ray crystallography and have been fitted into the 3D-reconstituted structure of the "extended" tail. The 3D structure of the "contracted" tail was also determined and interpreted in terms of component proteins. Given the pseudo-atomic tail structures both before and after contraction, it is now possible to understand the gross conformational change of the baseplate in terms of the change in the relative positions of the subunit proteins. These studies have explained how the conformational change of the baseplate and contraction of the tail are related to the tail's host cell recognition and membrane penetration function. On the other hand, the baseplate assembly process has been recently reexamined in detail in a precise system involving recombinant proteins (unlike the earlier studies with phage mutants). These experiments showed that the sequential association of the subunits of the baseplate wedge is based on the induced-fit upon association of each subunit. It was also found that, upon association of gp53 (gene product 53), the penultimate subunit of the wedge, six of the wedge intermediates spontaneously associate to form a baseplate-like structure in the absence of the central hub. Structure determination of the rest of the subunits and intermediate complexes and the assembly of the hub still require further study. BioMed Central 2010-12-03 /pmc/articles/PMC3004832/ /pubmed/21129200 http://dx.doi.org/10.1186/1743-422X-7-355 Text en Copyright ©2010 Leiman et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<url>http://creativecommons.org/licenses/by/2.0</url>), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Leiman, Petr G Arisaka, Fumio van Raaij, Mark J Kostyuchenko, Victor A Aksyuk, Anastasia A Kanamaru, Shuji Rossmann, Michael G Morphogenesis of the T4 tail and tail fibers |
title | Morphogenesis of the T4 tail and tail fibers |
title_full | Morphogenesis of the T4 tail and tail fibers |
title_fullStr | Morphogenesis of the T4 tail and tail fibers |
title_full_unstemmed | Morphogenesis of the T4 tail and tail fibers |
title_short | Morphogenesis of the T4 tail and tail fibers |
title_sort | morphogenesis of the t4 tail and tail fibers |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3004832/ https://www.ncbi.nlm.nih.gov/pubmed/21129200 http://dx.doi.org/10.1186/1743-422X-7-355 |
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