Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications
The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage ΦX174. The F protein forms a T = 1 capsid whose major folding motif is the eight–stranded antiparallelβ barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating...
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Veröffentlicht in: | Nature (London) 1992-01, Vol.355 (6356), p.137-143 |
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creator | McKenna, Robert Xia, Di Willingmann, Peter IIag, Leodevico L. Krishnaswamy, S. Rossmann, Michael G. Olson, Norman H. Baker, Timothy S. Incardona, Nino L. |
description | The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage ΦX174. The F protein forms a
T
= 1 capsid whose major folding motif is the eight–stranded antiparallelβ barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating spikes that enclose a hydrophilic channel containing some diffuse electron density. Each G protein is a tight β barrel with its strands running radially outwards and with a topology similar to that of the F protein. The 12 'pilot' H proteins per virion may be partially located in the putative ion channel. The small, basic J protein is associated with the DNA and is situated in an interior cleft of the F protein. Tentatively, there are three regions of partially ordered DNA structure, accounting for about 12% of the total genome. |
doi_str_mv | 10.1038/355137a0 |
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T
= 1 capsid whose major folding motif is the eight–stranded antiparallelβ barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating spikes that enclose a hydrophilic channel containing some diffuse electron density. Each G protein is a tight β barrel with its strands running radially outwards and with a topology similar to that of the F protein. The 12 'pilot' H proteins per virion may be partially located in the putative ion channel. The small, basic J protein is associated with the DNA and is situated in an interior cleft of the F protein. Tentatively, there are three regions of partially ordered DNA structure, accounting for about 12% of the total genome.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/355137a0</identifier><identifier>PMID: 1370343</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Bacteriophage phi X 174 - chemistry ; Bacteriophage phi X 174 - genetics ; Bacteriophage phi X 174 - ultrastructure ; Capsid - chemistry ; DNA, Viral - chemistry ; DNA, Viral - metabolism ; electron microscopy ; Humanities and Social Sciences ; Ion Channels - chemistry ; Ion Channels - metabolism ; Molecular Sequence Data ; Molecular Structure ; multidisciplinary ; Mutation ; phage Phi X174 ; Protein Conformation ; Science ; Science (multidisciplinary) ; structure ; Viral Proteins - chemistry ; Viral Structural Proteins - chemistry ; Viral Structural Proteins - genetics ; Viral Structural Proteins - metabolism ; X-Ray Diffraction</subject><ispartof>Nature (London), 1992-01, Vol.355 (6356), p.137-143</ispartof><rights>Springer Nature Limited 1992</rights><rights>1992 Nature Publishing Group 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c432t-4fd20a9e6bf28b1cf8a37266c2bd7eac04a15be4374bcb7b956067af6b45fa23</citedby><cites>FETCH-LOGICAL-c432t-4fd20a9e6bf28b1cf8a37266c2bd7eac04a15be4374bcb7b956067af6b45fa23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/355137a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/355137a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1370343$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McKenna, Robert</creatorcontrib><creatorcontrib>Xia, Di</creatorcontrib><creatorcontrib>Willingmann, Peter</creatorcontrib><creatorcontrib>IIag, Leodevico L.</creatorcontrib><creatorcontrib>Krishnaswamy, S.</creatorcontrib><creatorcontrib>Rossmann, Michael G.</creatorcontrib><creatorcontrib>Olson, Norman H.</creatorcontrib><creatorcontrib>Baker, Timothy S.</creatorcontrib><creatorcontrib>Incardona, Nino L.</creatorcontrib><title>Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage ΦX174. The F protein forms a
T
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Tentatively, there are three regions of partially ordered DNA structure, accounting for about 12% of the total genome.</description><subject>Amino Acid Sequence</subject><subject>Bacteriophage phi X 174 - chemistry</subject><subject>Bacteriophage phi X 174 - genetics</subject><subject>Bacteriophage phi X 174 - ultrastructure</subject><subject>Capsid - chemistry</subject><subject>DNA, Viral - chemistry</subject><subject>DNA, Viral - metabolism</subject><subject>electron microscopy</subject><subject>Humanities and Social Sciences</subject><subject>Ion Channels - chemistry</subject><subject>Ion Channels - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>multidisciplinary</subject><subject>Mutation</subject><subject>phage Phi X174</subject><subject>Protein Conformation</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>structure</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Structural Proteins - chemistry</subject><subject>Viral Structural Proteins - genetics</subject><subject>Viral Structural Proteins - metabolism</subject><subject>X-Ray Diffraction</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctKBSEAhiWKOl2gFwhcRS2mdHTUNsHhdIWoTYsWgaijJ2NmPOlM0Av1OD1THk5XWrQS_T5-fvwB2MboACMiDklVYcIVWgIjTDkrKBN8GYwQKkWBBGFrYD2lR4RQhTldBatZRoSSEbgf96H1BqY-DqYfooXBweS7aWOL_Ka62tbw5HoMtTK9jT7MHtTUwrfXuxwEM4a-T9ANnel96FQDfTtrvFHzW9oEK041yW59nBvg9uz0dnJRXN2cX07GV4WhpOwL6uoSqSPLtCuFxsYJRXjJmCl1za0yiCpcaUsJp9poro8qhhhXjmlaOVWSDXC8iJ0NurW1sV0u3shZ9K2KLzIoL3-Tzj_IaXiWFDPOBM4Bux8BMTwNNvWy9cnYplGdDUOSvORUZPVfETMiOEFzcW8hmhhSitZ9tcFIzheTn4tldedn-29xMVHm-wueMummNsrHMMT81elv1js9k6BQ</recordid><startdate>19920109</startdate><enddate>19920109</enddate><creator>McKenna, Robert</creator><creator>Xia, Di</creator><creator>Willingmann, Peter</creator><creator>IIag, Leodevico L.</creator><creator>Krishnaswamy, S.</creator><creator>Rossmann, Michael G.</creator><creator>Olson, Norman H.</creator><creator>Baker, Timothy S.</creator><creator>Incardona, Nino L.</creator><general>Nature Publishing Group UK</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>7QL</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19920109</creationdate><title>Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications</title><author>McKenna, Robert ; 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T
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subjects | Amino Acid Sequence Bacteriophage phi X 174 - chemistry Bacteriophage phi X 174 - genetics Bacteriophage phi X 174 - ultrastructure Capsid - chemistry DNA, Viral - chemistry DNA, Viral - metabolism electron microscopy Humanities and Social Sciences Ion Channels - chemistry Ion Channels - metabolism Molecular Sequence Data Molecular Structure multidisciplinary Mutation phage Phi X174 Protein Conformation Science Science (multidisciplinary) structure Viral Proteins - chemistry Viral Structural Proteins - chemistry Viral Structural Proteins - genetics Viral Structural Proteins - metabolism X-Ray Diffraction |
title | Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications |
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