Multidomain structure and correlated dynamics determined by self-consistent FRET networks.
Nat Methods
; 14(2): 174-180, 2017 02.
Article
em En
| MEDLINE
| ID: mdl-27918541
ABSTRACT
We present an approach that enables us to simultaneously access structure and dynamics of a multidomain protein in solution. Dynamic domain arrangements are experimentally determined by combining self-consistent networks of distance distributions with known domain structures. Local structural dynamics are correlated with the global arrangements by analyzing networks of time-resolved single-molecule fluorescence parameters. The strength of this hybrid approach is shown by an application to the flexible multidomain protein Hsp90. The average solution structure of Hsp90's closed state resembles the known X-ray crystal structure with Angstrom precision. The open state is represented by an ensemble of conformations with interdomain fluctuations of up to 25 Å. The data reveal a state-specific suppression of the submillisecond fluctuations by dynamic protein-protein interaction. Finally, the method enables localization and functional characterization of dynamic elements and domain interfaces.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Choque Térmico HSP90
/
Transferência Ressonante de Energia de Fluorescência
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Simulação de Dinâmica Molecular
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article