Examination of ClpB Quaternary Structure and Linkage to Nucleotide Binding.

@article{Lin2016ExaminationOC,
  title={Examination of ClpB Quaternary Structure and Linkage to Nucleotide Binding.},
  author={Jiabei Lin and Aaron L Lucius},
  journal={Biochemistry},
  year={2016},
  volume={55 12},
  pages={
          1758-71
        }
}
Escherichia coli caseinolytic peptidase B (ClpB) is a molecular chaperone with the unique ability to catalyze protein disaggregation in collaboration with the KJE system of chaperones. Like many AAA+ molecular motors, ClpB assembles into hexameric rings, and this reaction is thermodynamically linked to nucleotide binding. Here we show that ClpB exists in a dynamic equilibrium of monomers, dimers, tetramers, and hexamers in the presence of both limiting and excess ATPγS. We find that ClpB… CONTINUE READING
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