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The interdomain motions in myosin subfragment 1.
Reshetnyak, Y K; Andreev, O A.
Afiliación
  • Reshetnyak YK; Department of Molecular Biology and Immunology, Institute for Cancer Research, University of North Texas Health Science Center at Fort Worth, 3500 Camp Bowie Blvd, Fort Worth, TX 76107, USA.
Biophys Chem ; 94(1-2): 41-6, 2001 Dec 11.
Article en En | MEDLINE | ID: mdl-11744189
The interdomain motions in myosin subfragment 1 (S1) were studied by steady-state and time-resolved fluorescence of tryptophan residues and N-(iodoacetyl)-N'-(5-sulfo-1-naphtyl)ethylenediamine (AEDANS) attached to Cys178 of alkali light chain 1 (A1) exchanged into S1. The efficiency of fluorescence resonance energy transfer (FRET) from tryptophan residues of motor domain to AEDANS at A1 decreased dramatically after addition of ATP to S1A1-AEDANS. The efficiency of FRET calculated from the crystal structure of chicken S1 corresponded to the experimental one measured in the presence of ATP. The results showed that AEDANS at Cys178 of A1 became more mobile and distant from the motor domain of S1 upon ATP binding. These findings led to the suggestion that a release of the products of ATP hydrolysis and power stroke might be associated with movement of light chain-binding domain towards the N-terminal domain of S1.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Subfragmentos de Miosina Límite: Animals Idioma: En Revista: Biophys Chem Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos
Buscar en Google
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Imprimir
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PubMed Links

Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Subfragmentos de Miosina Límite: Animals Idioma: En Revista: Biophys Chem Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos