The dynamin A ring complex: molecular organization and nucleotide-dependent conformational changes.

@article{Klockow2002TheDA,
  title={The dynamin A ring complex: molecular organization and nucleotide-dependent conformational changes.},
  author={Boris Klockow and Willem Tichelaar and Dean R. Madden and Hartmut H. Niemann and Toshihiko Akiba and Keiko Hirose and Dietmar J Manstein},
  journal={The EMBO journal},
  year={2002},
  volume={21 3},
  pages={240-50}
}
Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self-assembles into rings and helices in a nucleotide-dependent manner, similar to human dynamin-1. Chemical modification of two cysteine residues, positioned in the middle domain and GTPase effector domain (GED), leads to altered assembly properties and the stabilization of a highly regular ring complex. Single particle analysis of this dynamin A* ring complex led to a three… CONTINUE READING

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Intermolecular and interdomain interactions of a dynamin-related GTP-binding protein, Dnm1p/Vps1p-like protein

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