SrasV1, Main, Exploration, bibRecord, 004588

The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties.

Identifieur interne : 004588 ( Main/Exploration ); précédent : 004587; suivant : 004589

The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties.

Auteurs : Hui Fan ; Amy Ooi ; Yong Wah Tan ; Sifang Wang ; Shouguo Fang ; Ding Xiang Liu ; Julien Lescar

Source :

Structure (London, England : 1993) [ 0969-2126 ] ; 2005.

RBID : pubmed:16338414

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Crystallography, Dimerization, Infectious bronchitis virus, Molecular Sequence Data, Nucleocapsid (chemistry), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Protein Structure, Tertiary, RNA (metabolism).
MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemistry : Nucleocapsid.
- chemical , metabolism : Nucleocapsid Proteins, RNA.
- Amino Acid Sequence, Crystallography, Dimerization, Infectious bronchitis virus, Molecular Sequence Data, Protein Structure, Tertiary.

Abstract

The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29-160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 A resolution reveals a protein core composed of a five-stranded antiparallel beta sheet with a positively charged beta hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation.

DOI: 10.1016/j.str.2005.08.021
PubMed: 16338414

Affiliations:

Le document en format XML

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<term>Molecular Sequence Data</term>
<term>Nucleocapsid (chemistry)</term>
<term>Nucleocapsid Proteins (chemistry)</term>
<term>Nucleocapsid Proteins (metabolism)</term>
<term>Protein Structure, Tertiary</term>
<term>RNA (metabolism)</term>
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<term>Protéines nucléocapside ()</term>
<term>Protéines nucléocapside (métabolisme)</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
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<term>Protéines nucléocapside</term>
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<term>Crystallography</term>
<term>Dimerization</term>
<term>Infectious bronchitis virus</term>
<term>Molecular Sequence Data</term>
<term>Protein Structure, Tertiary</term>
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<term>Données de séquences moléculaires</term>
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<term>Protéines nucléocapside</term>
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<front><div type="abstract" xml:lang="en">The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29-160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 A resolution reveals a protein core composed of a five-stranded antiparallel beta sheet with a positively charged beta hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation.</div>
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The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties.

The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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