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Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry
The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T...
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Published in: | Proceedings of the National Academy of Sciences - PNAS 2012-08, Vol.109 (35), p.14001-14006 |
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description | The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a φ 29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages. |
doi_str_mv | 10.1073/pnas.1207730109 |
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The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a φ 29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. 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Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.</description><subject>Appendages</subject><subject>Bacteria</subject><subject>Bacteriophages</subject><subject>Biological Sciences</subject><subject>Capsid</subject><subject>Capsid - chemistry</subject><subject>Capsid - ultrastructure</subject><subject>Capsid proteins</subject><subject>Capsid Proteins - chemistry</subject><subject>Cell walls</subject><subject>Cells</subject><subject>coat proteins</subject><subject>cryo-electron microscopy</subject><subject>Cryoelectron Microscopy</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>DNA</subject><subject>genome</subject><subject>Genomes</subject><subject>Myoviridae</subject><subject>Myoviridae - growth & development</subject><subject>Myoviridae - ultrastructure</subject><subject>Podoviridae</subject><subject>Podoviridae - growth & development</subject><subject>Podoviridae - ultrastructure</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>sequence homology</subject><subject>Siphoviridae</subject><subject>Streptococcus</subject><subject>Streptococcus - virology</subject><subject>Streptococcus Phages - growth & development</subject><subject>Streptococcus Phages - ultrastructure</subject><subject>structural proteins</subject><subject>Viral Structural Proteins - chemistry</subject><subject>Virus Replication - physiology</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNpdkc-P1CAcxYnRuOPo2ZNK4sWD3eULtJSLiZn4K9lEk3XPhFI6w6QtFegk-99Ld8ZZ9QKH93kPvt-H0Esgl0AEu5pGHS-BEiEYASIfoVU-oai4JI_RihAqippTfoGexbgnhMiyJk_RBaW1BCrLFZpuUphNmoPusRsPNia31cn5MWLfYY1_-NYfXHCttjimYKfkjTdmjnja6a3FG3iP3TD1zpxcnQ847SwerNnp0cVhyckJOd-OKdw9R0863Uf74nSv0e3nTz83X4vr71--bT5eF6YEmQroOG-rtpGdhIYAa5iQpO7AVFrLqjElBSHqBqADYF1DeQtl3ZRQt2VLKWFsjT4cc6e5GWxrlsd1r6bgBh3ulNdO_auMbqe2_qAYZzlG5oB3p4Dgf815MWpw0di-16P1c1RAmKCciXv07X_o3s9hzOPdU4zTqqozdXWkTPAxBtudPwNELW2qpU310GZ2vP57hjP_p74M4BOwOB_ipGKlAk7y4tbo1RHZx-TDmeEgCFSMZv3NUe-0V3obXFS3NzRr2UwlFzX7DTrhudg</recordid><startdate>20120828</startdate><enddate>20120828</enddate><creator>Aksyuk, Anastasia A</creator><creator>Bowman, Valorie D</creator><creator>Kaufmann, Bärbel</creator><creator>Fields, Christopher</creator><creator>Klose, Thomas</creator><creator>Holdaway, Heather A</creator><creator>Fischetti, Vincent A</creator><creator>Rossmann, Michael G</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120828</creationdate><title>Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry</title><author>Aksyuk, Anastasia A ; 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The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a φ 29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>22891295</pmid><doi>10.1073/pnas.1207730109</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Appendages Bacteria Bacteriophages Biological Sciences Capsid Capsid - chemistry Capsid - ultrastructure Capsid proteins Capsid Proteins - chemistry Cell walls Cells coat proteins cryo-electron microscopy Cryoelectron Microscopy Crystal structure Crystallography, X-Ray DNA genome Genomes Myoviridae Myoviridae - growth & development Myoviridae - ultrastructure Podoviridae Podoviridae - growth & development Podoviridae - ultrastructure Protein Structure, Tertiary Proteins sequence homology Siphoviridae Streptococcus Streptococcus - virology Streptococcus Phages - growth & development Streptococcus Phages - ultrastructure structural proteins Viral Structural Proteins - chemistry Virus Replication - physiology Viruses |
title | Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry |
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