SrasV1, Main, Exploration, bibRecord, 003B80

Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nspl5 suggests a role for hexamerization as an allosteric switch

Identifieur interne : 003B80 ( Main/Exploration ); précédent : 003B79; suivant : 003B81

Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nspl5 suggests a role for hexamerization as an allosteric switch

Auteurs : Jeremiah S. Joseph [États-Unis] ; KUMAR SINGH SAIKATENDU [États-Unis] ; Vanitha Subramanian [États-Unis] ; Benjamin W. Neuman [États-Unis] ; Michael J. Buchmeier [États-Unis] ; Raymond C. Stevens [États-Unis] ; Peter Kuhn [États-Unis]

Source :

Journal of virology [ 0022-538X ] ; 2007.

RBID : Pascal:07-0315436

Descripteurs français

KwdFr :
- Animaux, Clonage moléculaire, Conformation des protéines, Conformation moléculaire, Cristallographie aux rayons X, Dimérisation, Domaine catalytique, Manganèse (), Mutagenèse, Protéines virales non structurales (), RNA replicase (), Site allostérique, Sites de fixation, Virus du SRAS (enzymologie), Xenopus laevis, Électrophorèse sur gel de polyacrylamide.
MESH :
- enzymologie : Virus du SRAS.
Pascal (Inist)
- Animaux, Clonage moléculaire, Conformation des protéines, Conformation moléculaire, Coronavirus, Cristallographie aux rayons X, Dimérisation, Domaine catalytique, Manganèse, Mutagenèse, Protéines virales non structurales, RNA replicase, Site allostérique, Sites de fixation, Structure cristalline, Virologie, Syndrome respiratoire aigu sévère, Xenopus laevis, Électrophorèse sur gel de polyacrylamide.

English descriptors

KwdEn :
- Allosteric Site, Animals, Binding Sites, Catalytic Domain, Cloning, Molecular, Coronavirus, Crystalline structure, Crystallography, X-Ray, Dimerization, Electrophoresis, Polyacrylamide Gel, Manganese (chemistry), Molecular Conformation, Mutagenesis, Protein Conformation, RNA Replicase (chemistry), SARS Virus (enzymology), Severe acute respiratory syndrome, Viral Nonstructural Proteins (chemistry), Virology, Xenopus laevis.
MESH :
- chemical , chemistry : Manganese, RNA Replicase, Viral Nonstructural Proteins.
- enzymology : SARS Virus.
- Allosteric Site, Animals, Binding Sites, Catalytic Domain, Cloning, Molecular, Crystallography, X-Ray, Dimerization, Electrophoresis, Polyacrylamide Gel, Molecular Conformation, Mutagenesis, Protein Conformation, Xenopus laevis.

Abstract

Mature nonstructural protein-15 (nspl5) from the severe acute respiratory syndrome coronavirus (SARS-CoV) contains a novel uridylate-specific Mn²⁺-dependent endoribonuclease (NendoU). Structure studies of the full-length form of the obligate hexameric enzyme from two CoVs, SARS-CoV and murine hepatitis virus, and its monomeric homologue, XendoU from Xenopus laevis, combined with mutagenesis studies have implicated several residues in enzymatic activity and the N-terminal domain as the major determinant of hexamerization. However, the tight link between hexamerization and enzyme activity in NendoUs has remained an enigma. Here, we report the structure of a trimmed, monomeric form of SARS-CoV nspl5 (residues 28 to 335) determined to a resolution of 2.9 Å. The catalytic loop (residues 234 to 249) with its two reactive histidines (His 234 and His 249) is dramatically flipped by ∼120° into the active site cleft. Furthermore, the catalytic nucleophile Lys 289 points in a diametrically opposite direction, a consequence of an outward displacement of the supporting loop (residues 276 to 295). In the full-length hexameric forms, these two loops are packed against each other and are stabilized by intimate intersubunit interactions. Our results support the hypothesis that absence of an adjacent monomer due to deletion of the hexamerization domain is the most likely cause for disruption of the active site, offering a structural basis for why only the hexameric form of this enzyme is active.

Affiliations:

États-Unis

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Site</term>
<term>Animals</term>
<term>Binding Sites</term>
<term>Catalytic Domain</term>
<term>Cloning, Molecular</term>
<term>Coronavirus</term>
<term>Crystalline structure</term>
<term>Crystallography, X-Ray</term>
<term>Dimerization</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Manganese (chemistry)</term>
<term>Molecular Conformation</term>
<term>Mutagenesis</term>
<term>Protein Conformation</term>
<term>RNA Replicase (chemistry)</term>
<term>SARS Virus (enzymology)</term>
<term>Severe acute respiratory syndrome</term>
<term>Viral Nonstructural Proteins (chemistry)</term>
<term>Virology</term>
<term>Xenopus laevis</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Clonage moléculaire</term>
<term>Conformation des protéines</term>
<term>Conformation moléculaire</term>
<term>Cristallographie aux rayons X</term>
<term>Dimérisation</term>
<term>Domaine catalytique</term>
<term>Manganèse ()</term>
<term>Mutagenèse</term>
<term>Protéines virales non structurales ()</term>
<term>RNA replicase ()</term>
<term>Site allostérique</term>
<term>Sites de fixation</term>
<term>Virus du SRAS (enzymologie)</term>
<term>Xenopus laevis</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<term>RNA Replicase</term>
<term>Viral Nonstructural Proteins</term>
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<term>Binding Sites</term>
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<term>Crystallography, X-Ray</term>
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<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Molecular Conformation</term>
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<term>Xenopus laevis</term>
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<front><div type="abstract" xml:lang="en">Mature nonstructural protein-15 (nspl5) from the severe acute respiratory syndrome coronavirus (SARS-CoV) contains a novel uridylate-specific Mn<sup>2+</sup>
-dependent endoribonuclease (NendoU). Structure studies of the full-length form of the obligate hexameric enzyme from two CoVs, SARS-CoV and murine hepatitis virus, and its monomeric homologue, XendoU from Xenopus laevis, combined with mutagenesis studies have implicated several residues in enzymatic activity and the N-terminal domain as the major determinant of hexamerization. However, the tight link between hexamerization and enzyme activity in NendoUs has remained an enigma. Here, we report the structure of a trimmed, monomeric form of SARS-CoV nspl5 (residues 28 to 335) determined to a resolution of 2.9 Å. The catalytic loop (residues 234 to 249) with its two reactive histidines (His 234 and His 249) is dramatically flipped by ∼120° into the active site cleft. Furthermore, the catalytic nucleophile Lys 289 points in a diametrically opposite direction, a consequence of an outward displacement of the supporting loop (residues 276 to 295). In the full-length hexameric forms, these two loops are packed against each other and are stabilized by intimate intersubunit interactions. Our results support the hypothesis that absence of an adjacent monomer due to deletion of the hexamerization domain is the most likely cause for disruption of the active site, offering a structural basis for why only the hexameric form of this enzyme is active.</div>
</front>
</TEI>
<affiliations><list><country><li>États-Unis</li>
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<tree><country name="États-Unis"><noRegion><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S." last="Joseph">Jeremiah S. Joseph</name>
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<name sortKey="Kumar Singh Saikatendu" sort="Kumar Singh Saikatendu" uniqKey="Kumar Singh Saikatendu" last="Kumar Singh Saikatendu">KUMAR SINGH SAIKATENDU</name>
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Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nspl5 suggests a role for hexamerization as an allosteric switch

Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nspl5 suggests a role for hexamerization as an allosteric switch

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Abstract

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