Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property.
Identifieur interne : 002B47 ( Main/Exploration ); précédent : 002B46; suivant : 002B48Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property.
Auteurs : Yvonne Piotrowski [Allemagne] ; Guido Hansen ; A Linda Boomaars-Van Der Zanden ; Eric J. Snijder ; Alexander E. Gorbalenya ; Rolf HilgenfeldSource :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2009.
Descripteurs français
- KwdFr :
- Adénosine diphosphate ribose (), Adénosine diphosphate ribose (analogues et dérivés), Adénosine diphosphate ribose (métabolisme), Alignement de séquences, Conformation des protéines, Coronavirus humain 229E (), Coronavirus humain 229E (génétique), Coronavirus humain 229E (métabolisme), Cristallographie aux rayons X, Données de séquences moléculaires, Liaison aux protéines (physiologie), Modèles moléculaires, Phosphoric monoester hydrolases (), Phosphoric monoester hydrolases (génétique), Phosphoric monoester hydrolases (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Séquence d'acides aminés, Virus de la bronchite infectieuse (), Virus de la bronchite infectieuse (génétique), Virus de la bronchite infectieuse (métabolisme), Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- analogues et dérivés : Adénosine diphosphate ribose.
- génétique : Coronavirus humain 229E, Phosphoric monoester hydrolases, Protéines virales non structurales, Virus de la bronchite infectieuse, Virus du SRAS.
- métabolisme : Adénosine diphosphate ribose, Coronavirus humain 229E, Phosphoric monoester hydrolases, Protéines virales non structurales, Virus de la bronchite infectieuse, Virus du SRAS.
- physiologie : Liaison aux protéines.
- Adénosine diphosphate ribose, Alignement de séquences, Conformation des protéines, Coronavirus humain 229E, Cristallographie aux rayons X, Données de séquences moléculaires, Modèles moléculaires, Phosphoric monoester hydrolases, Protéines virales non structurales, Séquence d'acides aminés, Virus de la bronchite infectieuse, Virus du SRAS.
English descriptors
- KwdEn :
- Adenosine Diphosphate Ribose (analogs & derivatives), Adenosine Diphosphate Ribose (chemistry), Adenosine Diphosphate Ribose (metabolism), Amino Acid Sequence, Coronavirus 229E, Human (chemistry), Coronavirus 229E, Human (genetics), Coronavirus 229E, Human (metabolism), Crystallography, X-Ray, Infectious bronchitis virus (chemistry), Infectious bronchitis virus (genetics), Infectious bronchitis virus (metabolism), Models, Molecular, Molecular Sequence Data, Phosphoric Monoester Hydrolases (chemistry), Phosphoric Monoester Hydrolases (genetics), Phosphoric Monoester Hydrolases (metabolism), Protein Binding (physiology), Protein Conformation, SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Sequence Alignment, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , analogs & derivatives : Adenosine Diphosphate Ribose.
- chemical , chemistry : Adenosine Diphosphate Ribose, Phosphoric Monoester Hydrolases, Viral Nonstructural Proteins.
- chemical , genetics : Phosphoric Monoester Hydrolases, Viral Nonstructural Proteins.
- chemical , metabolism : Adenosine Diphosphate Ribose, Phosphoric Monoester Hydrolases, Viral Nonstructural Proteins.
- chemistry : Coronavirus 229E, Human, Infectious bronchitis virus, SARS Virus.
- genetics : Coronavirus 229E, Human, Infectious bronchitis virus, SARS Virus.
- metabolism : Coronavirus 229E, Human, Infectious bronchitis virus, SARS Virus.
- physiology : Protein Binding.
- Amino Acid Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Alignment.
Abstract
The polyproteins of coronaviruses are cleaved by viral proteases into at least 15 nonstructural proteins (Nsps). Consisting of five domains, Nsp3 is the largest of these (180-210 kDa). Among these domains, the so-called X-domain is believed to act as ADP-ribose-1''-phosphate phosphatase or to bind poly(ADP-ribose). However, here we show that the X-domain of Infectious Bronchitis Virus (strain Beaudette), a Group-3 coronavirus, fails to bind ADP-ribose. This is explained on the basis of the crystal structure of the protein, determined at two different pH values. For comparison, we also describe the crystal structure of the homologous X-domain from Human Coronavirus 229E, a Group-1 coronavirus, which does bind ADP-ribose.
DOI: 10.1002/pro.15
PubMed: 19177346
Affiliations:
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Le document en format XML
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virus (metabolism)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Phosphoric Monoester Hydrolases (chemistry)</term><term>Phosphoric Monoester Hydrolases (genetics)</term><term>Phosphoric Monoester Hydrolases (metabolism)</term><term>Protein Binding (physiology)</term><term>Protein Conformation</term><term>SARS Virus (chemistry)</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>Sequence Alignment</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adénosine diphosphate ribose ()</term><term>Adénosine diphosphate ribose (analogues et dérivés)</term><term>Adénosine diphosphate ribose (métabolisme)</term><term>Alignement de séquences</term><term>Conformation des protéines</term><term>Coronavirus humain 229E ()</term><term>Coronavirus humain 229E (génétique)</term><term>Coronavirus humain 229E (métabolisme)</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines (physiologie)</term><term>Modèles moléculaires</term><term>Phosphoric monoester hydrolases ()</term><term>Phosphoric monoester hydrolases (génétique)</term><term>Phosphoric monoester hydrolases (métabolisme)</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (génétique)</term><term>Protéines virales non structurales (métabolisme)</term><term>Séquence d'acides aminés</term><term>Virus de la bronchite infectieuse ()</term><term>Virus de la bronchite infectieuse (génétique)</term><term>Virus de la bronchite infectieuse (métabolisme)</term><term>Virus du SRAS ()</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Adenosine 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scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adénosine diphosphate ribose</term><term>Alignement de séquences</term><term>Conformation des protéines</term><term>Coronavirus humain 229E</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Phosphoric monoester hydrolases</term><term>Protéines virales non structurales</term><term>Séquence d'acides aminés</term><term>Virus de la bronchite infectieuse</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The polyproteins of coronaviruses are cleaved by viral proteases into at least 15 nonstructural proteins (Nsps). Consisting of five domains, Nsp3 is the largest of these (180-210 kDa). Among these domains, the so-called X-domain is believed to act as ADP-ribose-1''-phosphate phosphatase or to bind poly(ADP-ribose). However, here we show that the X-domain of Infectious Bronchitis Virus (strain Beaudette), a Group-3 coronavirus, fails to bind ADP-ribose. This is explained on the basis of the crystal structure of the protein, determined at two different pH values. For comparison, we also describe the crystal structure of the homologous X-domain from Human Coronavirus 229E, a Group-1 coronavirus, which does bind ADP-ribose.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Boomaars Van Der Zanden, A Linda" sort="Boomaars Van Der Zanden, A Linda" uniqKey="Boomaars Van Der Zanden A" first="A Linda" last="Boomaars-Van Der Zanden">A Linda Boomaars-Van Der Zanden</name><name sortKey="Gorbalenya, Alexander E" sort="Gorbalenya, Alexander E" uniqKey="Gorbalenya A" first="Alexander E" last="Gorbalenya">Alexander E. Gorbalenya</name><name sortKey="Hansen, Guido" sort="Hansen, Guido" uniqKey="Hansen G" first="Guido" last="Hansen">Guido Hansen</name><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name><name sortKey="Snijder, Eric J" sort="Snijder, Eric J" uniqKey="Snijder E" first="Eric J" last="Snijder">Eric J. Snijder</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Piotrowski, Yvonne" sort="Piotrowski, Yvonne" uniqKey="Piotrowski Y" first="Yvonne" last="Piotrowski">Yvonne Piotrowski</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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