X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.

@article{Fisher1995XraySO,
  title={X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.},
  author={Andrew J. Fisher and C. A. Dale Smith and James B. Thoden and R P Smith and Kazuo Sutoh and Hazel M. Holden and Ivan Rayment},
  journal={Biochemistry},
  year={1995},
  volume={34 28},
  pages={
          8960-72
        }
}
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 at 2.0 and 2.6 A resolution, respectively. Crystals of the beryllium fluoride-MgADP complex belong to space group P2(1)2(1)2 with unit cell parameters of a = 105.3 A, b = 182.6 A, and c = 54.7 A, whereas the crystals of the aluminum fluoride complex belong to the orthorhombic space group C222(1) with unit cell… 

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X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution.

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

The crystallized protein is enzymatically active in solution, indicating that the conformation of myosin observed in chicken skeletal myosIn subfragment-1 is unable to hydrolyze ATP and most likely represents the pre-hydrolysis structure for the myOSin head that occurs after release from actin.

Solution properties of full length and truncated forms of myosin subfragment 1 from Dictyostelium discoideum

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ATPase kinetics of the Dictyostelium discoideum myosin II motor domain

It is shown that the elementary steps of the S1dC ATPase pathway and the effects of actin are similar to those of the complete myosin head fragment, which indicates that truncation at residue E759, with the removal of the light chain binding sites, is not crucial to catalytic activity.

Formation and characterization of kinesin.ADP.fluorometal complexes.

The results suggest that these ternary complexes may mimic transient state intermediates in the kinesin ATPase cycle.

Solution structure of myosin-ADP-MgFn ternary complex by fluorescent probes and small-angle synchrotron X-ray scattering.

The results suggest that the overall conformation and localized functional regions of the complex are quite similar to those in the presence of ATP, indicating that the complex mimics the M(**).ADP.P(i) steady state.
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