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Literature summary for 5.6.1.8 extracted from

  • Logvinova, D.S.; Markov, D.I.; Nikolaeva, O.P.; Sluchanko, N.N.; Ushakov, D.S.; Levitsky, D.I.
    Does interaction between the motor and regulatory domains of the myosin head occur during ATPase cycle? Evidence from thermal unfolding studies on myosin subfragment 1 (2015), PLoS ONE, 10, e0137517.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of structures of nucleotide-free chicken skeletal S1 (PDB entry 2MYS) and chicken gizzard S1 in the S1-ADP-BeFx complex (PDB entry 1BR4) Gallus gallus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + myosin bound to actin filament at position n Gallus gallus
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ADP + phosphate + myosin bound to actin filament at position n+1
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additional information Gallus gallus myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (or catalytic) domain and the regulatory domain. Functioning of the myosin head as a molecular motor is believed to involve a rotation of the regulatory domain (lever arm) relative to the motor domain during the ATPase cycle. This rotation can be accompanied by an interaction between the motor domain and the C-terminus of the essential light chain associated with the regulatory domain. During rotation, the regulatory domain acts as a semi-rigid lever arm, which amplifies and transmits conformational changes occurring in the motor domain during ATP hydrolysis, the sliding velocity of actin filaments in the in vitro motility assay strongly depends on the length of the lever arm. The essential light chain associated with the regulatory domain may play a crucial role in the motor function of the myosin head, taking part in the overall stabilization of the S1 molecule during the ATPase cycle ?
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Organism

Organism UniProt Comment Textmining
Gallus gallus P13538 and P02609 and P02604
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Source Tissue

Source Tissue Comment Organism Textmining
muscle
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Gallus gallus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + myosin bound to actin filament at position n
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Gallus gallus ADP + phosphate + myosin bound to actin filament at position n+1
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?
additional information myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (or catalytic) domain and the regulatory domain. Functioning of the myosin head as a molecular motor is believed to involve a rotation of the regulatory domain (lever arm) relative to the motor domain during the ATPase cycle. This rotation can be accompanied by an interaction between the motor domain and the C-terminus of the essential light chain associated with the regulatory domain. During rotation, the regulatory domain acts as a semi-rigid lever arm, which amplifies and transmits conformational changes occurring in the motor domain during ATP hydrolysis, the sliding velocity of actin filaments in the in vitro motility assay strongly depends on the length of the lever arm. The essential light chain associated with the regulatory domain may play a crucial role in the motor function of the myosin head, taking part in the overall stabilization of the S1 molecule during the ATPase cycle Gallus gallus ?
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?

Subunits

Subunits Comment Organism
More domain structure of myosin head or myosin subfragment 1, S1 Gallus gallus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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thermal unfolding of myosin head or myosin subfragment 1, S1, thermally induced dissociation of leight chain 1 from the S1 heavy chain, overview Gallus gallus

General Information

General Information Comment Organism
additional information formation of the ternary complexes S1-ADP-AlF4 - and S1-ADP-BeFx that mimic S1 ATPase intermediate states S1-ADP-Pi and S1-ATP, respectively, and analysis of the changes in thermal unfolding and the domain structure. Local conformational changes in the myosin ATPase site spread to the entire motor domain, resulting in global structural changes in the motor domain. destabilizing of the regulatory domain by removal of essential light chain or regulatory light chain (and especially of both) markedly reduces the sliding velocity of actin filaments without a significant loss in actin-activated ATPase activity of myosin. the essential light chain associated with the regulatory domain may play a crucial role in the motor function of the myosin head, taking part in the overall stabilization of the S1 molecule during the ATPase cycle. Proposed interactions between the C-terminal half of essential light chain and the motor domain of the myosin head Gallus gallus
physiological function the molecular mechanism of muscle contraction and many other events of biological motility is based on cyclic interaction of myosin heads with actin filaments coupled to myosin-catalyzed ATP hydrolysis. The myosin head or myosin subfragment 1 consists of two major structural domains, the N-terminal globular motor (or catalytic) domain and the C-terminal regulatory domain. The motor domain is responsible for ATP hydrolysis and actin binding, modeling, overview Gallus gallus