X-ray Structures of the Apo and MgATP-bound States ofDictyostelium discoideum Myosin Motor Domain*

@article{Bauer2000XraySO,
  title={X-ray Structures of the Apo and MgATP-bound States ofDictyostelium discoideum Myosin Motor Domain*},
  author={C. Bauer and H. Holden and J. Thoden and R. Smith and I. Rayment},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={38494 - 38499}
}
Myosin is the most comprehensively studied molecular motor that converts energy from the hydrolysis of MgATP into directed movement. Its motile cycle consists of a sequential series of interactions between myosin, actin, MgATP, and the products of hydrolysis, where the affinity of myosin for actin is modulated by the nature of the nucleotide bound in the active site. The first step in the contractile cycle occurs when ATP binds to actomyosin and releases myosin from the complex. We report here… Expand
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TLDR
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References

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X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain.
The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myosin II (S1dC) complexed with MgAMPPNP, MgATPgammaS, and MgADP are reported at 2.1, 1.9, and 2.1 AExpand
X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.
TLDR
The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myOSin II complexed with beryllium and aluminum fluoride and magnesium ADP are reported, indicating that myos in undergoes a conformational change during hydrolysis that is not associated with the nucleotide binding pocket but rather occurs in the COOH-terminal segment of the myosIn motor domain. Expand
X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution.
TLDR
BeFx complex with S1Dc suggests that the conformational change, which occurs when ATP binds to actomyosin and which reduces the affinity of myosin for actin, is caused by the binding of the gamma- and beta-phosphate groups of the nucleotide. Expand
X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution.
The structure of the vanadate-trapped ADP complex of a truncated head of Dictyostelium myosin II consisting of residues Asp 2-Asn 762 has been determined by molecular replacement at 1.9 A resolutionExpand
Dictyostelium discoideum myosin II: characterization of functional myosin motor fragments.
TLDR
It is shown that C-terminal extension of M761 with one or two alpha-actinin repeats has very little effect on the behavior of the protein, making it an ideal construct for systematic studies of the structure, kinetics, and function of the myosin motor. Expand
Crystal Structure of a Vertebrate Smooth Muscle Myosin Motor Domain and Its Complex with the Essential Light Chain Visualization of the Pre–Power Stroke State
TLDR
A comparison of the lever arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a potential displacement of approximately 10 nm can be achieved during the power stroke, consistent with the fact that they both bind weakly to actin. Expand
Atomic Structure of Scallop Myosin Subfragment S1 Complexed with MgADP A Novel Conformation of the Myosin Head
TLDR
The crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 A resolution and reveals an unusual conformation of theMyosin head, which is believed to represent one of the prehydrolysis ("ATP") states of the contractile cycle in which the myOSin heads stay detached from actin. Expand
Mechanism for coupling free energy in ATPase to the myosin active site.
TLDR
In both the fiber and S1, it appears that the 6-position amino group of the bases of ADP and CDP is required to properly anchor the nucleotide in the active site, possibly at tyrosine 135 as suggested by X-ray crystallographic studies. Expand
X-ray Structures of the Dictyostelium discoideumMyosin Motor Domain with Six Non-nucleotide Analogs*
TLDR
A comparison of the kinetic and structural properties of the nanologs relative to ATP suggests that the ability of a substrate to sustain tension and to generate movement correlates with a well defined interaction with the active site water structure observed in S1dC·MgADP·BeF x . Expand
Use of stable analogs of myosin ATPase intermediates for kinetic studies of the "weak" binding of myosin heads to F-actin.
TLDR
The stable ternary complexes S1 x ADP x BeFx and S1xADP x AlF4- can be successfully used for kinetic studies of the "weak" binding of the myosin heads to F-actin. Expand
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