SrasV1, PubMed, Curation, bibRecord, 001972

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 : 001972 ( PubMed/Curation ); précédent : 001971; suivant : 001973

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.

Auteurs : Yvonne Piotrowski [Allemagne] ; Guido Hansen ; A Linda Boomaars-Van Der Zanden ; Eric J. Snijder ; Alexander E. Gorbalenya ; Rolf Hilgenfeld

Source :

Protein science : a publication of the Protein Society [ 1469-896X ] ; 2009.

RBID : pubmed:19177346

Descripteurs français

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

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Le document en format XML

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<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>
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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.

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.

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