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={A. Fisher and C. A. Smith and J. Thoden and R. Smith and K. Sutoh and H. Holden and I. 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… 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 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
X-ray Structures of the Apo and MgATP-bound States ofDictyostelium discoideum Myosin Motor Domain*
TLDR
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. Expand
Nucleotide and actin binding properties of the isolated motor domain from Dictyostelium discoideum myosin
TLDR
The results show that the nucleotide and actin binding of S1dC and subfragment 1 are similar but there are some differences in nucleophile and phosphate analogue-induced changes and the communication between the nucleotides andActin binding sites in these proteins. Expand
Solution properties of full length and truncated forms of myosin subfragment 1 from Dictyostelium discoideum
TLDR
Taken together, the results identify both truncation-caused differences between S1dC and flS1, as well as isoform-related differences between skeletal and Dictyostelium S1. Expand
ATPase kinetics of the Dictyostelium discoideum myosin II motor domain
TLDR
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. Expand
Structure of the regulatory domain of scallop myosin at 2 A resolution: implications for regulation.
TLDR
A model for regulation is proposed in which the Ca(2+)-bound RD is a rigid structure, and transient flexibility of the Ca-free RD allows the myosin heads to make stabilizing intramolecular linkage which shut off the motor. Expand
Formation and characterization of kinesin.ADP.fluorometal complexes.
TLDR
The results suggest that these ternary complexes may mimic transient state intermediates in the kinesin ATPase cycle. Expand
Evidence against essential roles for subdomain 1 of actin in actomyosin sliding movements.
We have engineered acto-S1chimera proteins carrying the entire actin inserted in loop 2 of the motor domain of Dictyostelium myosin II with 24 or 18 residue-linkers (CP24 and CP18, respectively).Expand
Solution structure of myosin-ADP-MgFn ternary complex by fluorescent probes and small-angle synchrotron X-ray scattering.
TLDR
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. Expand
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TLDR
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