Nuclear Magnetic Resonance Structure Shows that the Severe Acute Respiratory Syndrome Coronavirus-Unique Domain Contains a Macrodomain Fold▿
Identifieur interne : 003067 ( Main/Exploration ); précédent : 003066; suivant : 003068Nuclear Magnetic Resonance Structure Shows that the Severe Acute Respiratory Syndrome Coronavirus-Unique Domain Contains a Macrodomain Fold▿
Auteurs : Amarnath Chatterjee ; Margaret A. Johnson ; Pedro Serrano ; Bill Pedrini ; Jeremiah S. Joseph ; Benjamin W. Neuman ; Kumar Saikatendu ; Michael J. Buchmeier ; Peter Kuhn ; Kurt WüthrichSource :
- Journal of Virology [ 0022-538X ] ; 2008.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : RNA Replicase, RNA-Binding Proteins, Viral Nonstructural Proteins.
- chemical , metabolism : RNA.
- chemistry : SARS Virus.
- Electrophoretic Mobility Shift Assay, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Binding, Protein Structure, Tertiary.
Abstract
The nuclear magnetic resonance (NMR) structure of a central segment of the previously annotated severe acute respiratory syndrome (SARS)-unique domain (SUD-M, for “middle of the SARS-unique domain”) in SARS coronavirus (SARS-CoV) nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1"-phosphatase nsp3b, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection.
Url:
DOI: 10.1128/JVI.01781-08
PubMed: 19052085
PubMed Central: 2643772
Affiliations:
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Johnson</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Serrano, Pedro" sort="Serrano, Pedro" uniqKey="Serrano P" first="Pedro" last="Serrano">Pedro Serrano</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Pedrini, Bill" sort="Pedrini, Bill" uniqKey="Pedrini B" first="Bill" last="Pedrini">Bill Pedrini</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S." last="Joseph">Jeremiah S. Joseph</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W." last="Neuman">Benjamin W. 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SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1"-phosphatase nsp3b, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J." last="Buchmeier">Michael J. Buchmeier</name><name sortKey="Chatterjee, Amarnath" sort="Chatterjee, Amarnath" uniqKey="Chatterjee A" first="Amarnath" last="Chatterjee">Amarnath Chatterjee</name><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A." last="Johnson">Margaret A. Johnson</name><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S." last="Joseph">Jeremiah S. Joseph</name><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W." last="Neuman">Benjamin W. Neuman</name><name sortKey="Pedrini, Bill" sort="Pedrini, Bill" uniqKey="Pedrini B" first="Bill" last="Pedrini">Bill Pedrini</name><name sortKey="Saikatendu, Kumar" sort="Saikatendu, Kumar" uniqKey="Saikatendu K" first="Kumar" last="Saikatendu">Kumar Saikatendu</name><name sortKey="Serrano, Pedro" sort="Serrano, Pedro" uniqKey="Serrano P" first="Pedro" last="Serrano">Pedro Serrano</name><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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