Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping
The cytoplasmic polyhedrosis virus (CPV) from the family Reoviridae belongs to a subgroup of "turreted" reoviruses, in which the mRNA capping activity occurs in a pentameric turret. We report a full atomic model of CPV built from a 3D density map obtained using cryoelectron microscopy. The...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2011-01, Vol.108 (4), p.1373-1378 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Cheng, Lingpeng Sun, Jingchen Zhang, Kai Mou, Zongjun Huang, Xiaoxing Ji, Gang Sun, Fei Zhang, Jingqiang Zhu, Ping Harrison, Stephen C. |
| description | The cytoplasmic polyhedrosis virus (CPV) from the family Reoviridae belongs to a subgroup of "turreted" reoviruses, in which the mRNA capping activity occurs in a pentameric turret. We report a full atomic model of CPV built from a 3D density map obtained using cryoelectron microscopy. The image data for the 3D reconstruction were acquired exclusively from a CCD camera. Our structure shows that the enzymatic domains of the pentameric turret of CPV are topologically conserved and that there are five unique channels connecting the guanylyltransferase and methyltransferase regions. This structural organization reveals how the channels guide nascent mRNA sequentially to guanylyltransferase, 7-Nmethyltransferase, and 2'-O-methyltransferase in the turret, undergoing the highly coordinated mRNA capping activity. Furthermore, by fitting the deduced amino acid sequence of the protein VP5 to 120 large protrusion proteins on the CPV capsid shell, we confirmed that this protrusion protein is encoded by CPV RNA segment 7. |
| doi_str_mv | 10.1073/pnas.1014995108 |
| format | Article |
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We report a full atomic model of CPV built from a 3D density map obtained using cryoelectron microscopy. The image data for the 3D reconstruction were acquired exclusively from a CCD camera. Our structure shows that the enzymatic domains of the pentameric turret of CPV are topologically conserved and that there are five unique channels connecting the guanylyltransferase and methyltransferase regions. This structural organization reveals how the channels guide nascent mRNA sequentially to guanylyltransferase, 7-Nmethyltransferase, and 2'-O-methyltransferase in the turret, undergoing the highly coordinated mRNA capping activity. Furthermore, by fitting the deduced amino acid sequence of the protein VP5 to 120 large protrusion proteins on the CPV capsid shell, we confirmed that this protrusion protein is encoded by CPV RNA segment 7.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1014995108</identifier><identifier>PMID: 21220303</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Sequence ; Amino acids ; Biological Sciences ; Capsid ; Capsid - metabolism ; Capsid - ultrastructure ; Capsid proteins ; Capsid Proteins - chemistry ; Capsid Proteins - genetics ; Capsid Proteins - ultrastructure ; Cells ; Cryoelectron Microscopy - methods ; Cypovirus ; Cytoplasmic polyhedrosis virus ; Messenger RNA ; Microscopy ; Models, Molecular ; Models, Structural ; Molecular Sequence Data ; Molecular Structure ; Orthoreovirus ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins ; Reoviridae ; Reoviridae - genetics ; Reoviridae - metabolism ; Reoviridae - ultrastructure ; RNA ; RNA Caps ; RNA, Messenger - genetics ; RNA, Viral - genetics ; Sequence Homology, Amino Acid ; Viral morphology ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2011-01, Vol.108 (4), p.1373-1378</ispartof><rights>Copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jan 25, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c496t-c45ab0d1f00f47c4a2e297b21186e4867485cf7138ecd1a0f4485ab2d9499c53</citedby><cites>FETCH-LOGICAL-c496t-c45ab0d1f00f47c4a2e297b21186e4867485cf7138ecd1a0f4485ab2d9499c53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/108/4.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41001868$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41001868$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21220303$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cheng, Lingpeng</creatorcontrib><creatorcontrib>Sun, Jingchen</creatorcontrib><creatorcontrib>Zhang, Kai</creatorcontrib><creatorcontrib>Mou, Zongjun</creatorcontrib><creatorcontrib>Huang, Xiaoxing</creatorcontrib><creatorcontrib>Ji, Gang</creatorcontrib><creatorcontrib>Sun, Fei</creatorcontrib><creatorcontrib>Zhang, Jingqiang</creatorcontrib><creatorcontrib>Zhu, Ping</creatorcontrib><creatorcontrib>Harrison, Stephen C.</creatorcontrib><title>Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The cytoplasmic polyhedrosis virus (CPV) from the family Reoviridae belongs to a subgroup of "turreted" reoviruses, in which the mRNA capping activity occurs in a pentameric turret. 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We report a full atomic model of CPV built from a 3D density map obtained using cryoelectron microscopy. The image data for the 3D reconstruction were acquired exclusively from a CCD camera. Our structure shows that the enzymatic domains of the pentameric turret of CPV are topologically conserved and that there are five unique channels connecting the guanylyltransferase and methyltransferase regions. This structural organization reveals how the channels guide nascent mRNA sequentially to guanylyltransferase, 7-Nmethyltransferase, and 2'-O-methyltransferase in the turret, undergoing the highly coordinated mRNA capping activity. Furthermore, by fitting the deduced amino acid sequence of the protein VP5 to 120 large protrusion proteins on the CPV capsid shell, we confirmed that this protrusion protein is encoded by CPV RNA segment 7.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>21220303</pmid><doi>10.1073/pnas.1014995108</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Amino acids Biological Sciences Capsid Capsid - metabolism Capsid - ultrastructure Capsid proteins Capsid Proteins - chemistry Capsid Proteins - genetics Capsid Proteins - ultrastructure Cells Cryoelectron Microscopy - methods Cypovirus Cytoplasmic polyhedrosis virus Messenger RNA Microscopy Models, Molecular Models, Structural Molecular Sequence Data Molecular Structure Orthoreovirus Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Proteins Reoviridae Reoviridae - genetics Reoviridae - metabolism Reoviridae - ultrastructure RNA RNA Caps RNA, Messenger - genetics RNA, Viral - genetics Sequence Homology, Amino Acid Viral morphology Viruses |
| title | Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping |
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