Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein.
Identifieur interne : 001F22 ( PubMed/Corpus ); précédent : 001F21; suivant : 001F23Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein.
Auteurs : Kumar Singh Saikatendu ; Jeremiah S. Joseph ; Vanitha Subramanian ; Benjamin W. Neuman ; Michael J. Buchmeier ; Raymond C. Stevens ; Peter KuhnSource :
- Journal of virology [ 0022-538X ] ; 2007.
English descriptors
- KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, Genome, Viral, Models, Molecular, Molecular Sequence Data, Nucleocapsid (chemistry), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, SARS Virus (chemistry), SARS Virus (metabolism), SARS Virus (physiology), Sequence Homology, Amino Acid, Viral Proteins (genetics).
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemistry : Nucleocapsid, SARS Virus.
- chemical , genetics : Viral Proteins.
- chemical , metabolism : Nucleocapsid Proteins, SARS Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Crystallography, X-Ray, Genome, Viral, Models, Molecular, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid.
Abstract
Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as oligomerization modules during assembly. The C terminus of the N protein anchors it to the viral membrane by associating with M protein. We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 A (monoclinic) and at 1.85 A (cubic), respectively, resolved by molecular replacement using the homologous avian infectious bronchitis virus (IBV) structure. Flexible loops in the solution structure of SARS-CoV N-NTD are now shown to be well ordered around the beta-sheet core. The functionally important positively charged beta-hairpin protrudes out of the core, is oriented similarly to that in the IBV N-NTD, and is involved in crystal packing in the monoclinic form. In the cubic form, the monomers form trimeric units that stack in a helical array. Comparison of crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA recognition, but they probably associate differently in vivo during the formation of the ribonucleoprotein complex. Electrostatic potential distribution on the surface of homology models of related coronaviral N-NTDs suggests that they use different modes of both RNA recognition and oligomeric assembly, perhaps explaining why their nucleocapsids have different morphologies.
DOI: 10.1128/JVI.02236-06
PubMed: 17229691
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pubmed:17229691Le document en format XML
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Joseph</name></author><author><name sortKey="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</name></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W" last="Neuman">Benjamin W. Neuman</name></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J" last="Buchmeier">Michael J. Buchmeier</name></author><author><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C" last="Stevens">Raymond C. Stevens</name></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17229691</idno><idno type="pmid">17229691</idno><idno type="doi">10.1128/JVI.02236-06</idno><idno type="wicri:Area/PubMed/Corpus">001F22</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001F22</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein.</title><author><name sortKey="Saikatendu, Kumar Singh" sort="Saikatendu, Kumar Singh" uniqKey="Saikatendu K" first="Kumar Singh" last="Saikatendu">Kumar Singh Saikatendu</name><affiliation><nlm:affiliation>Department of Cell Biology, 10550 N. Torrey Pines Rd., CB265, The Scripps Research Institute, La Jolla, CA 92037, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S" last="Joseph">Jeremiah S. Joseph</name></author><author><name sortKey="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</name></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W" last="Neuman">Benjamin W. Neuman</name></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J" last="Buchmeier">Michael J. Buchmeier</name></author><author><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C" last="Stevens">Raymond C. Stevens</name></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Genome, Viral</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Nucleocapsid (chemistry)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>SARS Virus (chemistry)</term><term>SARS Virus (metabolism)</term><term>SARS Virus (physiology)</term><term>Sequence Homology, Amino Acid</term><term>Viral Proteins (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid</term><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Genome, Viral</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Sequence Homology, Amino Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as oligomerization modules during assembly. The C terminus of the N protein anchors it to the viral membrane by associating with M protein. We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 A (monoclinic) and at 1.85 A (cubic), respectively, resolved by molecular replacement using the homologous avian infectious bronchitis virus (IBV) structure. Flexible loops in the solution structure of SARS-CoV N-NTD are now shown to be well ordered around the beta-sheet core. The functionally important positively charged beta-hairpin protrudes out of the core, is oriented similarly to that in the IBV N-NTD, and is involved in crystal packing in the monoclinic form. In the cubic form, the monomers form trimeric units that stack in a helical array. Comparison of crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA recognition, but they probably associate differently in vivo during the formation of the ribonucleoprotein complex. Electrostatic potential distribution on the surface of homology models of related coronaviral N-NTDs suggests that they use different modes of both RNA recognition and oligomeric assembly, perhaps explaining why their nucleocapsids have different morphologies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17229691</PMID><DateCompleted><Year>2007</Year><Month>05</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>27</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>81</Volume><Issue>8</Issue><PubDate><Year>2007</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein.</ArticleTitle><Pagination><MedlinePgn>3913-21</MedlinePgn></Pagination><Abstract><AbstractText>Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as oligomerization modules during assembly. The C terminus of the N protein anchors it to the viral membrane by associating with M protein. We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 A (monoclinic) and at 1.85 A (cubic), respectively, resolved by molecular replacement using the homologous avian infectious bronchitis virus (IBV) structure. Flexible loops in the solution structure of SARS-CoV N-NTD are now shown to be well ordered around the beta-sheet core. The functionally important positively charged beta-hairpin protrudes out of the core, is oriented similarly to that in the IBV N-NTD, and is involved in crystal packing in the monoclinic form. In the cubic form, the monomers form trimeric units that stack in a helical array. Comparison of crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA recognition, but they probably associate differently in vivo during the formation of the ribonucleoprotein complex. Electrostatic potential distribution on the surface of homology models of related coronaviral N-NTDs suggests that they use different modes of both RNA recognition and oligomeric assembly, perhaps explaining why their nucleocapsids have different morphologies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Saikatendu</LastName><ForeName>Kumar Singh</ForeName><Initials>KS</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, 10550 N. 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HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:17229691" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |