Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter.

@article{Orelle2010DynamicsOA,
  title={Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter.},
  author={C{\'e}dric Orelle and Frances J D Alvarez and Michael L. Oldham and Arnaud Orelle and Theodore E Wiley and Jue Chen and Amy L. Davidson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 47},
  pages={20293-8}
}
ATP-binding cassette (ABC) transporters are powered by a nucleotide-binding domain dimer that opens and closes during cycles of ATP hydrolysis. These domains consist of a RecA-like subdomain and an α-helical subdomain that is specific to the family. Many studies on isolated domains suggest that the helical subdomain rotates toward the RecA-like subdomain in response to ATP binding, moving the family signature motif into a favorable position to interact with the nucleotide across the dimer… CONTINUE READING

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