Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3
Identifieur interne : 001251 ( Ncbi/Curation ); précédent : 001250; suivant : 001252Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3
Auteurs : Kumar Singh Saikatendu ; Jeremiah S. Joseph ; Vanitha Subramanian ; Tom Clayton ; Mark Griffith ; Kin Moy ; Jeffrey Velasquez ; Benjamin W. Neuman ; Michael J. Buchmeier ; Raymond C. Stevens ; Peter KuhnSource :
- Structure (London, England : 1993) [ 0969-2126 ] ; 2005.
Descripteurs français
- KwdFr :
- Adénosine diphosphate ribose (analogues et dérivés), Adénosine diphosphate ribose (métabolisme), Analyse de séquence de protéine, Données de séquences moléculaires, Phosphorylation, Protéines virales non structurales (), Protéines virales non structurales (physiologie), RNA replicase (), RNA replicase (physiologie), Relation structure-activité, Structure tertiaire des protéines (physiologie), Séquence conservée (physiologie), Séquence d'acides aminés, Virus du SRAS (), Virus du SRAS (enzymologie), Virus du SRAS (physiologie).
- MESH :
- analogues et dérivés : Adénosine diphosphate ribose.
- enzymologie : Virus du SRAS.
- métabolisme : Adénosine diphosphate ribose.
- physiologie : Protéines virales non structurales, RNA replicase, Structure tertiaire des protéines, Séquence conservée, Virus du SRAS.
- Analyse de séquence de protéine, Données de séquences moléculaires, Phosphorylation, Protéines virales non structurales, RNA replicase, Relation structure-activité, Séquence d'acides aminés, Virus du SRAS.
English descriptors
- KwdEn :
- Adenosine Diphosphate Ribose (analogs & derivatives), Adenosine Diphosphate Ribose (metabolism), Amino Acid Sequence, Conserved Sequence (physiology), Molecular Sequence Data, Phosphorylation, Protein Structure, Tertiary (physiology), RNA Replicase (chemistry), RNA Replicase (physiology), SARS Virus (chemistry), SARS Virus (enzymology), SARS Virus (physiology), Sequence Analysis, Protein, Structure-Activity Relationship, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (physiology).
- MESH :
- chemical , analogs & derivatives : Adenosine Diphosphate Ribose.
- chemical , chemistry : RNA Replicase, Viral Nonstructural Proteins.
- chemical , metabolism : Adenosine Diphosphate Ribose.
- chemistry : SARS Virus.
- enzymology : SARS Virus.
- physiology : Conserved Sequence, Protein Structure, Tertiary, RNA Replicase, SARS Virus, Viral Nonstructural Proteins.
- Amino Acid Sequence, Molecular Sequence Data, Phosphorylation, Sequence Analysis, Protein, Structure-Activity Relationship.
Abstract
The crystal structure of a conserved domain of nonstructural protein 3 (nsP3) from severe acute respiratory syndrome coronavirus (SARS-CoV) has been solved by single-wavelength anomalous dispersion to 1.4 Å resolution. The structure of this “X” domain, seen in many single-stranded RNA viruses, reveals a three-layered α/β/α core with a macro-H2A-like fold. The putative active site is a solvent-exposed cleft that is conserved in its three structural homologs, yeast Ymx7,
Url:
DOI: 10.1016/j.str.2005.07.022
PubMed: 16271890
PubMed Central: 7126892
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PMC:7126892Le 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="Clayton, Tom" sort="Clayton, Tom" uniqKey="Clayton T" first="Tom" last="Clayton">Tom Clayton</name></author><author><name sortKey="Griffith, Mark" sort="Griffith, Mark" uniqKey="Griffith M" first="Mark" last="Griffith">Mark Griffith</name></author><author><name sortKey="Moy, Kin" sort="Moy, Kin" uniqKey="Moy K" first="Kin" last="Moy">Kin Moy</name></author><author><name sortKey="Velasquez, Jeffrey" sort="Velasquez, Jeffrey" uniqKey="Velasquez J" first="Jeffrey" last="Velasquez">Jeffrey Velasquez</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">Structure (London, England : 1993)</title><idno type="ISSN">0969-2126</idno><idno type="eISSN">1878-4186</idno><imprint><date when="2005">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Diphosphate Ribose (analogs & derivatives)</term><term>Adenosine Diphosphate Ribose (metabolism)</term><term>Amino Acid Sequence</term><term>Conserved Sequence (physiology)</term><term>Molecular Sequence Data</term><term>Phosphorylation</term><term>Protein Structure, Tertiary (physiology)</term><term>RNA Replicase (chemistry)</term><term>RNA Replicase (physiology)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (enzymology)</term><term>SARS Virus (physiology)</term><term>Sequence Analysis, Protein</term><term>Structure-Activity Relationship</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adénosine diphosphate ribose (analogues et dérivés)</term><term>Adénosine diphosphate ribose (métabolisme)</term><term>Analyse de séquence de protéine</term><term>Données de séquences moléculaires</term><term>Phosphorylation</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (physiologie)</term><term>RNA replicase ()</term><term>RNA replicase (physiologie)</term><term>Relation structure-activité</term><term>Structure tertiaire des protéines (physiologie)</term><term>Séquence conservée (physiologie)</term><term>Séquence d'acides aminés</term><term>Virus du SRAS ()</term><term>Virus du SRAS (enzymologie)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Adenosine Diphosphate Ribose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Diphosphate Ribose</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Adénosine diphosphate ribose</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adénosine diphosphate ribose</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines virales non structurales</term><term>RNA replicase</term><term>Structure tertiaire des protéines</term><term>Séquence conservée</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Conserved Sequence</term><term>Protein Structure, Tertiary</term><term>RNA Replicase</term><term>SARS Virus</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Phosphorylation</term><term>Sequence Analysis, Protein</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence de protéine</term><term>Données de séquences moléculaires</term><term>Phosphorylation</term><term>Protéines virales non structurales</term><term>RNA replicase</term><term>Relation structure-activité</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Summary</title><p>The crystal structure of a conserved domain of nonstructural protein 3 (nsP3) from severe acute respiratory syndrome coronavirus (SARS-CoV) has been solved by single-wavelength anomalous dispersion to 1.4 Å resolution. The structure of this “X” domain, seen in many single-stranded RNA viruses, reveals a three-layered α/β/α core with a macro-H2A-like fold. The putative active site is a solvent-exposed cleft that is conserved in its three structural homologs, yeast Ymx7, <italic>Archeoglobus fulgidus</italic> AF1521, and Er58 from <italic>E. coli</italic>. Its sequence is similar to yeast YBR022W (also known as Poa1P), a known phosphatase that acts on ADP-ribose-1″-phosphate (Appr-1″-p). The SARS nsP3 domain readily removes the 1″ phosphate group from Appr-1″-p in in vitro assays, confirming its phosphatase activity. Sequence and structure comparison of all known macro-H2A domains combined with available functional data suggests that proteins of this superfamily form an emerging group of nucleotide phosphatases that dephosphorylate Appr-1″-p.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Allen, M D" uniqKey="Allen M">M.D. Allen</name></author><author><name sortKey="Buckle, A M" uniqKey="Buckle A">A.M. Buckle</name></author><author><name sortKey="Cordell, S C" uniqKey="Cordell S">S.C. Cordell</name></author><author><name sortKey="Lowe, J" uniqKey="Lowe J">J. Lowe</name></author><author><name sortKey="Bycroft, M" uniqKey="Bycroft M">M. Bycroft</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Altschul, S F" uniqKey="Altschul S">S.F. Altschul</name></author><author><name sortKey="Madden, T L" uniqKey="Madden T">T.L. Madden</name></author><author><name sortKey="Schaffer, A A" uniqKey="Schaffer A">A.A. 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Ziebuhr</name></author><author><name sortKey="Thiel, V" uniqKey="Thiel V">V. Thiel</name></author><author><name sortKey="Gorbalenya, A E" uniqKey="Gorbalenya A">A.E. Gorbalenya</name></author></analytic></biblStruct></listBibl></div1></back></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/RBID.i -Sk "pubmed:16271890" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |