A Novel Restricted Photoaffinity Spin-Labeled Non-Nucleoside ATP Analogue as a Covalently Attached Reporter Group of the Active Site of Myosin Subfragment 1†

Biochemistry ◽  
2002 ◽  
Vol 41 (8) ◽  
pp. 2609-2620 ◽  
Author(s):  
Xiaoru Chen ◽  
Jean Grammer ◽  
J. David Lawson ◽  
Roger Cooke ◽  
Edward Pate ◽  
...  
Keyword(s):  
Active Site ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Reporter Group

Characterization of the properties of ethenoadenosine nucleotides bound or trapped at the active site of myosin subfragment 1

Biochemistry ◽  
1984 ◽  
Vol 23 (17) ◽  
pp. 3994-4002 ◽  
Author(s):  
William J. Perkins ◽  
James A. Wells ◽  
Ralph G. Yount
Keyword(s):  
Active Site ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

scholarly journals The Role of Magnesium in Binding of the Nucleotide Polyphosphate Chain to the Active Site of Myosin Subfragment-1

1983 ◽  
Vol 134 (2) ◽  
pp. 197-204 ◽  
Author(s):  
Marcus C. SCHAUB ◽  
John G. WATTERSON ◽  
Klaus LOTH ◽  
Daniela FOLETTA
Keyword(s):  
Active Site ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

scholarly journals Regulation of the acto·myosin subfragment 1 interaction by troponin/tropomyosin. Evidence for control of a specific isomerization between two acto·myosin subfragment 1 states

1991 ◽  
Vol 279 (3) ◽  
pp. 711-718 ◽  
Author(s):  
D F A McKillop ◽  
M A Geeves
Keyword(s):  
Skeletal Muscle ◽  
Active Site ◽  
Actin Filaments ◽  
Thin Filaments ◽  
Closed State ◽  
Myosin Subfragment ◽  
Actomyosin Interaction ◽  
Binding Isotherms ◽  
Myosin Subfragment 1 ◽  
Site Binding

The co-operative binding of myosin subfragment 1 (S1) to reconstituted skeletal-muscle thin filaments has been examined by monitoring the fluorescence of a pyrene probe on Cys-374 of actin. The degree of co-operativity differs when phosphate, sulphate or ADP are bound to the S1 active site. Binding isotherms have been analysed according to the Geeves & Halsall [(1987) Biophys. J. 52, 215-220] model, which proposed that troponin and tropomyosin effected regulation of the actomyosin interaction by controlling an isomerization of the actomyosin complex. The data support the proposal that seven actin monomers associated with a single tropomyosin molecule act as a co-operative unit that can be in one of two states. In the ‘closed’ state myosin can bind to actin, but the subsequent isomerization is prevented. The isomerization is only allowed after the seven-actin unit is in the ‘open’ form. Ca2+ controls the proportion of actin filaments in the ‘closed’ and ‘open’ forms in the absence of myosin heads. The ratio of ‘closed’ to ‘open’ forms is approx. 50:1 in the absence of Ca2+ and 5:1 in its presence.

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