Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU.

@article{Wang2001NucleotidedependentCC,
  title={Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU.},
  author={Jimin Wang and Jae Jun Song and Ihn Sik Seong and Matthew C. Franklin and Satwik Kamtekar and Soo Hyun Eom and Chin Ha Chung},
  journal={Structure},
  year={2001},
  volume={9 11},
  pages={1107-16}
}
BACKGROUND The bacterial heat shock locus ATPase HslU is an AAA(+) protein that has structures known in many nucleotide-free and -bound states. Nucleotide is required for the formation of the biologically active HslU hexameric assembly. The hexameric HslU ATPase binds the dodecameric HslV peptidase and forms an ATP-dependent HslVU protease. RESULTS We have characterized four distinct HslU conformational states, going sequentially from open to closed: the empty, SO(4), ATP, and ADP states. The… CONTINUE READING
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