Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirus.
Identifieur interne : 002442 ( Main/Exploration ); précédent : 002441; suivant : 002443Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirus.
Auteurs : Yanlin Ma [République populaire de Chine] ; Xiaohang Tong ; Xiaoling Xu ; Xuemei Li ; Zhiyong Lou ; Zihe RaoSource :
- Protein & cell [ 1674-8018 ] ; 2010.
Descripteurs français
- KwdFr :
- ARN (métabolisme), Alignement de séquences, Cristallographie aux rayons X, Données de séquences moléculaires, Liaison aux protéines, Multimérisation de protéines, Phosphoprotéines (), Phosphoprotéines (métabolisme), Pliage des protéines, Protéines nucléocapside (), Protéines nucléocapside (métabolisme), Sites de fixation, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Virus de l'hépatite murine (), Virus de l'hépatite murine (métabolisme).
- MESH :
- métabolisme : ARN, Phosphoprotéines, Protéines nucléocapside, Virus de l'hépatite murine.
- Alignement de séquences, Cristallographie aux rayons X, Données de séquences moléculaires, Liaison aux protéines, Multimérisation de protéines, Phosphoprotéines, Pliage des protéines, Protéines nucléocapside, Sites de fixation, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Virus de l'hépatite murine.
English descriptors
- KwdEn :
- Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Molecular Sequence Data, Murine hepatitis virus (chemistry), Murine hepatitis virus (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Phosphoproteins (chemistry), Phosphoproteins (metabolism), Protein Binding, Protein Folding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, RNA (metabolism), Sequence Alignment.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins, Phosphoproteins.
- chemistry : Murine hepatitis virus.
- metabolism : Murine hepatitis virus, Nucleocapsid Proteins, Phosphoproteins, RNA.
- Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Molecular Sequence Data, Protein Binding, Protein Folding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment.
Abstract
Coronaviruses are the causative agent of respiratory and enteric diseases in animals and humans. One example is SARS, which caused a worldwide health threat in 2003. In coronaviruses, the structural protein N (nucleocapsid protein) associates with the viral RNA to form the filamentous nucleocapsid and plays a crucial role in genome replication and transcription. The structure of N-terminal domain of MHV N protein also implicated its specific affinity with transcriptional regulatory sequence (TRS) RNA. Here we report the crystal structures of the two proteolytically resistant N- (NTD) and C-terminal (CTD) domains of the N protein from murine hepatitis virus (MHV). The structure of NTD in two different crystal forms was solved to 1.5 Å. The higher resolution provides more detailed structural information than previous reports, showing that the NTD structure from MHV shares a similar overall and topology structure with that of SARS-CoV and IBV, but varies in its potential surface, which indicates a possible difference in RNA-binding module. The structure of CTD was solved to 2.0-Å resolution and revealed a tightly intertwined dimer. This is consistent with analytical ultracentrifugation experiments, suggesting a dimeric assembly of the N protein. The similarity between the structures of these two domains from SARS-CoV, IBV and MHV corroborates a conserved mechanism of nucleocapsid formation for coronaviruses.
DOI: 10.1007/s13238-010-0079-x
PubMed: 21203940
Affiliations:
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Le document en format XML
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One example is SARS, which caused a worldwide health threat in 2003. In coronaviruses, the structural protein N (nucleocapsid protein) associates with the viral RNA to form the filamentous nucleocapsid and plays a crucial role in genome replication and transcription. The structure of N-terminal domain of MHV N protein also implicated its specific affinity with transcriptional regulatory sequence (TRS) RNA. Here we report the crystal structures of the two proteolytically resistant N- (NTD) and C-terminal (CTD) domains of the N protein from murine hepatitis virus (MHV). The structure of NTD in two different crystal forms was solved to 1.5 Å. The higher resolution provides more detailed structural information than previous reports, showing that the NTD structure from MHV shares a similar overall and topology structure with that of SARS-CoV and IBV, but varies in its potential surface, which indicates a possible difference in RNA-binding module. The structure of CTD was solved to 2.0-Å resolution and revealed a tightly intertwined dimer. This is consistent with analytical ultracentrifugation experiments, suggesting a dimeric assembly of the N protein. 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