Overlap between folding and functional energy landscapes for adenylate kinase conformational change.

@article{Olsson2010OverlapBF,
  title={Overlap between folding and functional energy landscapes for adenylate kinase conformational change.},
  author={Ulrika Olsson and Magnus Wolf-Watz},
  journal={Nature communications},
  year={2010},
  volume={1},
  pages={111}
}
Enzyme function is often dependent on fluctuations between inactive and active structural ensembles. Adenylate kinase isolated from Escherichia coli (AK(e)) is a small phosphotransfer enzyme in which interconversion between inactive (open) and active (closed) conformations is rate limiting for catalysis. AK(e) has a modular three-dimensional architecture with two flexible substrate-binding domains that interact with the substrates AMP, ADP and ATP. Here, we show by using a combination of… CONTINUE READING

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