Dynamic reorganization of the motor domain of myosin subfragment 1 in different nucleotide states

Emoke Bódis, Krisztina Szarka, M. Nyitrai, B. Somogyi

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Atomic models of the myosin motor domain with different bound nucleotides have revealed the open and closed conformations of the switch 2 element [Geeves, M. A. & Holmes, K.C. (1999) Annu. Rev. Biochem. 68, 687-728]. The two conformations are in dynamic equilibrium, which is controlled by the bound nucleotide. In the present work we attempted to characterize the flexibility of the motor domain in the open and closed conformations in rabbit skeletal myosin subfragment 1. Three residues (Ser181, Lys553 and Cys707) were labelled with fluorophores and the probes identified three fluorescence resonance energy transfer pairs. The effect of ADP, ADP.BeFx, ADP.AlF4 - and ADP.Vi on the conformation of the motor domain was shown by applying temperature-dependent fluorescence resonance energy transfer methods. The 50 kDa lower domain was found to maintain substantial rigidity in both the open and closed conformations to provide the structural basis of the interaction of myosin with actin. The flexibility of the 50 kDa upper domain was high in the open conformation and further increased in the closed conformation. The converter region of subfragment 1 became more rigid during the open-to-closed transition, the conformational change of which can provide the mechanical basis of the energy transduction from the nucleotide-binding pocket to the light-chain-binding domain.

Original languageEnglish
Pages (from-to)4835-4845
Number of pages11
JournalEuropean Journal of Biochemistry
Volume270
Issue number24
DOIs
Publication statusPublished - Dec 2003

Fingerprint

Myosin Subfragments
Adenosine Diphosphate
Conformations
Fluorescence Resonance Energy Transfer
Nucleotides
Myosins
Actins
Rabbits
Light
Temperature
Fluorophores
Rigidity
Switches

Keywords

  • Fluorescence resonance energy transfer
  • Muscle
  • Myosin
  • Nucleotides
  • Protein dynamics and conformation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Dynamic reorganization of the motor domain of myosin subfragment 1 in different nucleotide states. / Bódis, Emoke; Szarka, Krisztina; Nyitrai, M.; Somogyi, B.

In: European Journal of Biochemistry, Vol. 270, No. 24, 12.2003, p. 4835-4845.

Research output: Contribution to journalArticle

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