Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.
Identifieur interne : 002458 ( PubMed/Curation ); précédent : 002457; suivant : 002459Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.
Auteurs : Kumar Singh Saikatendu [États-Unis] ; 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 A resolution. The structure of this "X" domain, seen in many single-stranded RNA viruses, reveals a three-layered alpha/beta/alpha 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, Archeoglobus fulgidus AF1521, and Er58 from E. coli. 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.
DOI: 10.1016/j.str.2005.07.022
PubMed: 16271890
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The structure of this "X" domain, seen in many single-stranded RNA viruses, reveals a three-layered alpha/beta/alpha 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, Archeoglobus fulgidus AF1521, and Er58 from E. coli. 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16271890</PMID><DateCompleted><Year>2008</Year><Month>07</Month><Day>10</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0969-2126</ISSN><JournalIssue CitedMedium="Print"><Volume>13</Volume><Issue>11</Issue><PubDate><Year>2005</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Structure (London, England : 1993)</Title><ISOAbbreviation>Structure</ISOAbbreviation></Journal><ArticleTitle>Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.</ArticleTitle><Pagination><MedlinePgn>1665-75</MedlinePgn></Pagination><Abstract><AbstractText>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 A resolution. The structure of this "X" domain, seen in many single-stranded RNA viruses, reveals a three-layered alpha/beta/alpha 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, Archeoglobus fulgidus AF1521, and Er58 from E. coli. 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Saikatendu</LastName><ForeName>Kumar Singh</ForeName><Initials>KS</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Joseph</LastName><ForeName>Jeremiah S</ForeName><Initials>JS</Initials></Author><Author ValidYN="Y"><LastName>Subramanian</LastName><ForeName>Vanitha</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Clayton</LastName><ForeName>Tom</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Griffith</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Moy</LastName><ForeName>Kin</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Velasquez</LastName><ForeName>Jeffrey</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Neuman</LastName><ForeName>Benjamin W</ForeName><Initials>BW</Initials></Author><Author ValidYN="Y"><LastName>Buchmeier</LastName><ForeName>Michael J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Stevens</LastName><ForeName>Raymond C</ForeName><Initials>RC</Initials></Author><Author ValidYN="Y"><LastName>Kuhn</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2ACF</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>HHSN 266200400058C</GrantID><Acronym>HS</Acronym><Agency>AHRQ HHS</Agency><Country>United 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1''-phosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>20762-30-5</RegistryNumber><NameOfSubstance UI="D000246">Adenosine Diphosphate Ribose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.48</RegistryNumber><NameOfSubstance UI="D012324">RNA Replicase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.48</RegistryNumber><NameOfSubstance UI="C510959">nonstructural protein 3, SARS coronovirus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Structure. 2005 Nov;13(11):1582-3</RefSource><PMID Version="1">16271880</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000246" MajorTopicYN="N">Adenosine Diphosphate Ribose</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012324" MajorTopicYN="N">RNA Replicase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020539" MajorTopicYN="N">Sequence Analysis, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000502" 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