A new pentameric structure of rotavirus NSP4 revealed by molecular replacement.
Acta Crystallogr D Biol Crystallogr
; 68(Pt 1): 57-61, 2012 Jan.
Article
em En
| MEDLINE
| ID: mdl-22194333
ABSTRACT
The region spanning residues 95-146 of the rotavirus nonstructural protein NSP4 from the asymptomatic human strain ST3 has been purified and crystallized and diffraction data have been collected to a resolution of 2.6 Å. Several attempts to solve the structure by the molecular-replacement method using the available tetrameric structures of this domain were unsuccessful despite a sequence identity of 73% to the already known structures. A more systematic approach with a dimer as the search model led to an unexpected pentameric structure using the program Phaser. The various steps involved in arriving at this molecular-replacement solution, which unravelled a case of subtle variation between different oligomeric states unknown at the time of solving the structure, are presented in this paper.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Toxinas Biológicas
/
Glicoproteínas
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Proteínas não Estruturais Virais
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Rotavirus
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Estrutura Quaternária de Proteína
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article