Literature DB >> 2958713

Location of the ATPase site of myosin determined by three-dimensional electron microscopy.

M Tokunaga1, K Sutoh, C Toyoshima, T Wakabayashi.   

Abstract

Both ATP hydrolysis by myosin and the accompanying cyclic association-dissociation of actin and myosin are essential for muscle contraction. It is important for understanding the molecular mechanism of contraction to know the three-dimensional locations of the two major functional sites of myosin: the ATPase site and the actin-binding site. We have determined the position of the ATPase site of myosin using three-dimensional image reconstruction from electron micrographs and site-specific labelling with the avidin-biotin system. The ATPase site is about 5 nm from the tip of the myosin head and is about 4 nm away from the actin-binding site of myosin. This is the first report of the three-dimensional location of an enzyme active site by electron microscopy.

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Year:  1987        PMID: 2958713     DOI: 10.1038/329635a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  25 in total

1.  Time-resolved X-ray diffraction by skinned skeletal muscle fibers during activation and shortening.

Authors:  B K Hoskins; C C Ashley; G Rapp; P J Griffiths
Journal:  Biophys J       Date:  2001-01       Impact factor: 4.033

2.  Frequency-dependent distortion of meridional intensity changes during sinusoidal length oscillations of activated skeletal muscle.

Authors:  M A Bagni; B Colombini; H Amenitsch; S Bernstorff; C C Ashley; G Rapp; P J Griffiths
Journal:  Biophys J       Date:  2001-06       Impact factor: 4.033

3.  Changes in myosin S1 orientation and force induced by a temperature increase.

Authors:  Peter J Griffiths; Maria A Bagni; Barbara Colombini; Heinz Amenitsch; Sigrid Bernstorff; Christopher C Ashley; Giovanni Cecchi; Heinz Ameritsch
Journal:  Proc Natl Acad Sci U S A       Date:  2002-04-16       Impact factor: 11.205

4.  Interhead distances in myosin attached to F-actin estimated by fluorescence energy transfer spectroscopy.

Authors:  S Ishiwata; M Miki; I Shin; T Funatsu; K Yasuda; C G dos Remedios
Journal:  Biophys J       Date:  1997-08       Impact factor: 4.033

Review 5.  Efficiency of muscle contraction. The chemimechanic equilibrium.

Authors:  E W Becker
Journal:  Naturwissenschaften       Date:  1991-10

6.  Molecular charge dominates the inhibition of actomyosin in skinned muscle fibers by SH1 peptides.

Authors:  P B Chase; T W Beck; J Bursell; M J Kushmerick
Journal:  Biophys J       Date:  1991-08       Impact factor: 4.033

Review 7.  Domains, motions and regulation in the myosin head.

Authors:  P Vibert; C Cohen
Journal:  J Muscle Res Cell Motil       Date:  1988-08       Impact factor: 2.698

8.  On the origin and transmission of force in actomyosin subfragment 1.

Authors:  J Botts; J F Thomason; M F Morales
Journal:  Proc Natl Acad Sci U S A       Date:  1989-04       Impact factor: 11.205

9.  Constraints on the attachment of myosin to actin.

Authors:  R Tregear
Journal:  J Muscle Res Cell Motil       Date:  1988-08       Impact factor: 2.698

10.  [2-3H]ATP synthesis and 3H NMR spectroscopy of enzyme-nucleotide complexes: ADP and ADP.Vi bound to myosin subfragment 1.

Authors:  S Highsmith; M Kubinec; D K Jaiswal; H Morimoto; P G Williams; D E Wemmer
Journal:  J Biomol NMR       Date:  1993-05       Impact factor: 2.835

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