The structure of an open state of beta-actin at 2.65 A resolution.

@article{Chik1996TheSO,
  title={The structure of an open state of beta-actin at 2.65 A resolution.},
  author={John K Chik and Uno Lindberg and Clarence Schutt},
  journal={Journal of molecular biology},
  year={1996},
  volume={263 4},
  pages={
          607-23
        }
}
The structure of an "open state" of crystalline profilin:beta-actin has been solved to 2.65 A by X-ray crystallography. The open-state crystals, in 1.8 M potassium phosphate, have an expanded unit cell dimension in the c direction of 185.7 A compared with 171.9 A in the previously solved ammonium sulphate-stabilized "tight-state" structure. The unit cell change between the open and the tight states is accompanied by large subdomain movements in actin. Furthermore, the nucleotide in the open… 

The open nucleotide pocket of the profilin/actin x-ray structure is unstable and closes in the absence of profilin.

Molecular dynamics simulations are used to model the thermodynamic properties of the actin x-ray structure, outside the crystal lattice, in an aqueous environment with profilin removed, and show that the open-nucleotide-pocket, Profilin-free structure is actually unstable, and closes.

Crystal Structure of Monomeric Actin in the ATP State

The x-ray crystal structure of tetramethylrhodamine-5-maleimide-actin with bound AMPPNP, a non-hydrolyzable ATP analog, was determined and an analysis of the existing structures of members of the actin superfamily suggests that the cleft is open in the nucleotide-free state.

ATPase activity and conformational changes in the regulation of actin.

  • H. Schüler
  • Chemistry, Biology
    Biochimica et biophysica acta
  • 2001

Structure and dynamics of calmodulin in solution.

Crystal Structures of Expressed Non-polymerizable Monomeric Actin in the ADP and ATP States*

This work expressed a cytoplasmic actin in Sf9 cells, which was rendered non-polymerizable by virtue of two point mutations in subdomain 4 (A204E/P243K), and suggests that the nucleotide-dependent formation of the D-loop helix may result from signal propagation through crystal packing interactions.

The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin.

A plausible model of F-actin can be constructed by reintroducing the known filament twist, without disturbing significantly the interface observed in the actin dimer crystal.

Solution properties of tetramethylrhodamine-modified G-actin.

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X‐ray structure analysis of actin and of the NH2‐terminal domain of the heat‐shock cognate protein Hsc70 has revealed an unexpected extensive structural similarity between these two molecules, suggesting that the molecules may have evolved by gene duplication.
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