The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins
The final step in the morphogenesis of long-tailed double-stranded DNA bacteriophages is the joining of the DNA-filled head to the tail. The connector is a specialized structure of the head that serves as the interface for tail attachment and the point of egress for DNA from the head during infectio...
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| Veröffentlicht in: | Journal of molecular biology 2010-01, Vol.395 (4), p.754-768 |
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| creator | Cardarelli, Lia Lam, Robert Tuite, Ashleigh Baker, Lindsay A. Sadowski, Paul D. Radford, Devon R. Rubinstein, John L. Battaile, Kevin P. Chirgadze, Nickolay Maxwell, Karen L. Davidson, Alan R. |
| description | The final step in the morphogenesis of long-tailed double-stranded DNA bacteriophages is the joining of the DNA-filled head to the tail. The connector is a specialized structure of the head that serves as the interface for tail attachment and the point of egress for DNA from the head during infection. Here, we report the determination of a 2.1 Å crystal structure of gp6 of bacteriophage HK97. Through structural comparisons, functional studies, and bioinformatic analysis, gp6 has been determined to be a component of the connector of phage HK97 that is evolutionarily related to gp15, a well-characterized connector component of bacteriophage SPP1. Whereas the structure of gp15 was solved in a monomeric form, gp6 crystallized as an oligomeric ring with the dimensions expected for a connector protein. Although this ring is composed of 13 subunits, which does not match the symmetry of the connector within the phage, sequence conservation and modeling of this structure into the cryo-electron microscopy density of the SPP1 connector indicate that this oligomeric structure represents the arrangement of gp6 subunits within the mature phage particle. Through sequence searches and genomic position analysis, we determined that gp6 is a member of a large family of connector proteins that are present in long-tailed phages. We have also identified gp7 of HK97 as a homologue of gp16 of phage SPP1, which is the second component of the connector of this phage. These proteins are members of another large protein family involved in connector assembly. |
| doi_str_mv | 10.1016/j.jmb.2009.10.067 |
| format | Article |
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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>The final step in the morphogenesis of long-tailed double-stranded DNA bacteriophages is the joining of the DNA-filled head to the tail. The connector is a specialized structure of the head that serves as the interface for tail attachment and the point of egress for DNA from the head during infection. Here, we report the determination of a 2.1 Å crystal structure of gp6 of bacteriophage HK97. Through structural comparisons, functional studies, and bioinformatic analysis, gp6 has been determined to be a component of the connector of phage HK97 that is evolutionarily related to gp15, a well-characterized connector component of bacteriophage SPP1. Whereas the structure of gp15 was solved in a monomeric form, gp6 crystallized as an oligomeric ring with the dimensions expected for a connector protein. Although this ring is composed of 13 subunits, which does not match the symmetry of the connector within the phage, sequence conservation and modeling of this structure into the cryo-electron microscopy density of the SPP1 connector indicate that this oligomeric structure represents the arrangement of gp6 subunits within the mature phage particle. Through sequence searches and genomic position analysis, we determined that gp6 is a member of a large family of connector proteins that are present in long-tailed phages. We have also identified gp7 of HK97 as a homologue of gp16 of phage SPP1, which is the second component of the connector of this phage. These proteins are members of another large protein family involved in connector assembly.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2009.10.067</identifier><identifier>PMID: 19895817</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Bacteria ; bacteriophage assembly ; BACTERIOPHAGES ; CONNECTORS ; CRYSTAL STRUCTURE ; Crystallography, X-Ray ; DIMENSIONS ; DNA ; FUNCTIONALS ; head–tail connector ; HK97 ; MATERIALS SCIENCE ; MICROSCOPY ; Microscopy, Electron, Transmission ; Models, Molecular ; Molecular Sequence Data ; MORPHOGENESIS ; Mutagenesis ; Phage HK97 ; Phage SPP1 ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Subunits ; PROTEINS ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - ultrastructure ; Sequence Homology, Amino Acid ; SIMULATION ; Siphoviridae - chemistry ; Siphoviridae - genetics ; Siphoviridae - physiology ; Siphoviridae - ultrastructure ; Static Electricity ; Structural Homology, Protein ; SYMMETRY ; Viral Proteins - chemistry ; Viral Proteins - genetics ; Viral Proteins - physiology ; Viral Proteins - ultrastructure ; Virus Assembly ; X-ray crystallography</subject><ispartof>Journal of molecular biology, 2010-01, Vol.395 (4), p.754-768</ispartof><rights>2009 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c477t-c67b2457a29a9b301f4f6c8c29b7762a3a233d2ea998183410a16a8f290f870b3</citedby><cites>FETCH-LOGICAL-c477t-c67b2457a29a9b301f4f6c8c29b7762a3a233d2ea998183410a16a8f290f870b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jmb.2009.10.067$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19895817$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1002249$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Cardarelli, Lia</creatorcontrib><creatorcontrib>Lam, Robert</creatorcontrib><creatorcontrib>Tuite, Ashleigh</creatorcontrib><creatorcontrib>Baker, Lindsay A.</creatorcontrib><creatorcontrib>Sadowski, Paul D.</creatorcontrib><creatorcontrib>Radford, Devon R.</creatorcontrib><creatorcontrib>Rubinstein, John L.</creatorcontrib><creatorcontrib>Battaile, Kevin P.</creatorcontrib><creatorcontrib>Chirgadze, Nickolay</creatorcontrib><creatorcontrib>Maxwell, Karen L.</creatorcontrib><creatorcontrib>Davidson, Alan R.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The final step in the morphogenesis of long-tailed double-stranded DNA bacteriophages is the joining of the DNA-filled head to the tail. The connector is a specialized structure of the head that serves as the interface for tail attachment and the point of egress for DNA from the head during infection. Here, we report the determination of a 2.1 Å crystal structure of gp6 of bacteriophage HK97. Through structural comparisons, functional studies, and bioinformatic analysis, gp6 has been determined to be a component of the connector of phage HK97 that is evolutionarily related to gp15, a well-characterized connector component of bacteriophage SPP1. Whereas the structure of gp15 was solved in a monomeric form, gp6 crystallized as an oligomeric ring with the dimensions expected for a connector protein. Although this ring is composed of 13 subunits, which does not match the symmetry of the connector within the phage, sequence conservation and modeling of this structure into the cryo-electron microscopy density of the SPP1 connector indicate that this oligomeric structure represents the arrangement of gp6 subunits within the mature phage particle. Through sequence searches and genomic position analysis, we determined that gp6 is a member of a large family of connector proteins that are present in long-tailed phages. We have also identified gp7 of HK97 as a homologue of gp16 of phage SPP1, which is the second component of the connector of this phage. These proteins are members of another large protein family involved in connector assembly.</description><subject>Amino Acid Sequence</subject><subject>Bacteria</subject><subject>bacteriophage assembly</subject><subject>BACTERIOPHAGES</subject><subject>CONNECTORS</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallography, X-Ray</subject><subject>DIMENSIONS</subject><subject>DNA</subject><subject>FUNCTIONALS</subject><subject>head–tail connector</subject><subject>HK97</subject><subject>MATERIALS SCIENCE</subject><subject>MICROSCOPY</subject><subject>Microscopy, Electron, Transmission</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>MORPHOGENESIS</subject><subject>Mutagenesis</subject><subject>Phage HK97</subject><subject>Phage SPP1</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Subunits</subject><subject>PROTEINS</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - ultrastructure</subject><subject>Sequence Homology, Amino Acid</subject><subject>SIMULATION</subject><subject>Siphoviridae - chemistry</subject><subject>Siphoviridae - genetics</subject><subject>Siphoviridae - physiology</subject><subject>Siphoviridae - ultrastructure</subject><subject>Static Electricity</subject><subject>Structural Homology, Protein</subject><subject>SYMMETRY</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - physiology</subject><subject>Viral Proteins - ultrastructure</subject><subject>Virus Assembly</subject><subject>X-ray crystallography</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2u0zAQhS0E4pYLD8AGWWxYpfgn9Q-soHApohJIlHXkOJPWURIX20HqjnfgDXkSHKUSO1hZ4_nOsWcOQk8pWVNCxctu3Q31mhGic70mQt5DK0qULpTg6j5aEcJYwRQXN-hRjB0hZMNL9RDdUK30RlG5Qt3hBHgbLjGZHn9NYbJpCoB9i98amyA4fz6ZI-DdJy3x8Sxe4XfQutGNR2zw3oTcujOD6y-zZAem-f3z18G4Hm_9OIJNPuAvwSdwY3yMHrSmj_Dket6ib3fvD9tdsf_84eP2zb6wpZSpsELWrNxIw7TRNSe0LVthlWW6llIwww3jvGFgtFZU8ZISQ4VRLdOkVZLU_BY9X3x9TK6K1iWwJ7t8p6LzTkqdoRcLdA7--wQxVYOLFvrejOCnWGnCeMn4hv-XlJkTjAmRSbqQNvgYA7TVObjBhEt-tZoDq7oqB1bNgc1XObCseXZ1n-oBmr-Ka0IZeL0AkFf2w0GYJ4LRQuPCPFDj3T_s_wBaTaRT</recordid><startdate>20100129</startdate><enddate>20100129</enddate><creator>Cardarelli, Lia</creator><creator>Lam, Robert</creator><creator>Tuite, Ashleigh</creator><creator>Baker, Lindsay A.</creator><creator>Sadowski, Paul D.</creator><creator>Radford, Devon R.</creator><creator>Rubinstein, John L.</creator><creator>Battaile, Kevin P.</creator><creator>Chirgadze, Nickolay</creator><creator>Maxwell, Karen L.</creator><creator>Davidson, Alan R.</creator><general>Elsevier Ltd</general><general>Elsevier</general><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>7X8</scope><scope>7T7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>OTOTI</scope></search><sort><creationdate>20100129</creationdate><title>The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins</title><author>Cardarelli, Lia ; Lam, Robert ; Tuite, Ashleigh ; Baker, Lindsay A. ; Sadowski, Paul D. ; Radford, Devon R. ; Rubinstein, John L. ; Battaile, Kevin P. ; Chirgadze, Nickolay ; Maxwell, Karen L. ; Davidson, Alan R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-c67b2457a29a9b301f4f6c8c29b7762a3a233d2ea998183410a16a8f290f870b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Bacteria</topic><topic>bacteriophage assembly</topic><topic>BACTERIOPHAGES</topic><topic>CONNECTORS</topic><topic>CRYSTAL STRUCTURE</topic><topic>Crystallography, X-Ray</topic><topic>DIMENSIONS</topic><topic>DNA</topic><topic>FUNCTIONALS</topic><topic>head–tail connector</topic><topic>HK97</topic><topic>MATERIALS SCIENCE</topic><topic>MICROSCOPY</topic><topic>Microscopy, Electron, Transmission</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>MORPHOGENESIS</topic><topic>Mutagenesis</topic><topic>Phage HK97</topic><topic>Phage SPP1</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Subunits</topic><topic>PROTEINS</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - ultrastructure</topic><topic>Sequence Homology, Amino Acid</topic><topic>SIMULATION</topic><topic>Siphoviridae - chemistry</topic><topic>Siphoviridae - genetics</topic><topic>Siphoviridae - physiology</topic><topic>Siphoviridae - ultrastructure</topic><topic>Static Electricity</topic><topic>Structural Homology, Protein</topic><topic>SYMMETRY</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - physiology</topic><topic>Viral Proteins - ultrastructure</topic><topic>Virus Assembly</topic><topic>X-ray crystallography</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cardarelli, Lia</creatorcontrib><creatorcontrib>Lam, Robert</creatorcontrib><creatorcontrib>Tuite, Ashleigh</creatorcontrib><creatorcontrib>Baker, Lindsay A.</creatorcontrib><creatorcontrib>Sadowski, Paul D.</creatorcontrib><creatorcontrib>Radford, Devon R.</creatorcontrib><creatorcontrib>Rubinstein, John L.</creatorcontrib><creatorcontrib>Battaile, Kevin P.</creatorcontrib><creatorcontrib>Chirgadze, Nickolay</creatorcontrib><creatorcontrib>Maxwell, Karen L.</creatorcontrib><creatorcontrib>Davidson, Alan R.</creatorcontrib><creatorcontrib>Argonne National Lab. 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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2010-01-29</date><risdate>2010</risdate><volume>395</volume><issue>4</issue><spage>754</spage><epage>768</epage><pages>754-768</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>The final step in the morphogenesis of long-tailed double-stranded DNA bacteriophages is the joining of the DNA-filled head to the tail. The connector is a specialized structure of the head that serves as the interface for tail attachment and the point of egress for DNA from the head during infection. Here, we report the determination of a 2.1 Å crystal structure of gp6 of bacteriophage HK97. Through structural comparisons, functional studies, and bioinformatic analysis, gp6 has been determined to be a component of the connector of phage HK97 that is evolutionarily related to gp15, a well-characterized connector component of bacteriophage SPP1. Whereas the structure of gp15 was solved in a monomeric form, gp6 crystallized as an oligomeric ring with the dimensions expected for a connector protein. Although this ring is composed of 13 subunits, which does not match the symmetry of the connector within the phage, sequence conservation and modeling of this structure into the cryo-electron microscopy density of the SPP1 connector indicate that this oligomeric structure represents the arrangement of gp6 subunits within the mature phage particle. Through sequence searches and genomic position analysis, we determined that gp6 is a member of a large family of connector proteins that are present in long-tailed phages. We have also identified gp7 of HK97 as a homologue of gp16 of phage SPP1, which is the second component of the connector of this phage. These proteins are members of another large protein family involved in connector assembly.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>19895817</pmid><doi>10.1016/j.jmb.2009.10.067</doi><tpages>15</tpages></addata></record> |
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| ispartof | Journal of molecular biology, 2010-01, Vol.395 (4), p.754-768 |
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| subjects | Amino Acid Sequence Bacteria bacteriophage assembly BACTERIOPHAGES CONNECTORS CRYSTAL STRUCTURE Crystallography, X-Ray DIMENSIONS DNA FUNCTIONALS head–tail connector HK97 MATERIALS SCIENCE MICROSCOPY Microscopy, Electron, Transmission Models, Molecular Molecular Sequence Data MORPHOGENESIS Mutagenesis Phage HK97 Phage SPP1 Protein Multimerization Protein Structure, Quaternary Protein Subunits PROTEINS Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - ultrastructure Sequence Homology, Amino Acid SIMULATION Siphoviridae - chemistry Siphoviridae - genetics Siphoviridae - physiology Siphoviridae - ultrastructure Static Electricity Structural Homology, Protein SYMMETRY Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - physiology Viral Proteins - ultrastructure Virus Assembly X-ray crystallography |
| title | The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins |
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