SERCA mutant E309Q binds two Ca(2+) ions but adopts a catalytically incompetent conformation.

@article{Clausen2013SERCAME,
  title={SERCA mutant E309Q binds two Ca(2+) ions but adopts a catalytically incompetent conformation.},
  author={Johannes D. Clausen and Maike Bublitz and Bertrand Arnou and C{\'e}dric Montigny and Christine Jaxel and Jesper Vuust M\oller and Poul Nissen and Jens P Andersen and Marc le Maire},
  journal={The EMBO journal},
  year={2013},
  volume={32 24},
  pages={3231-43}
}
The sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) couples ATP hydrolysis to transport of Ca(2+). This directed energy transfer requires cross-talk between the two Ca(2+) sites and the phosphorylation site over 50 Å distance. We have addressed the mechano-structural basis for this intramolecular signal by analysing the structure and the functional properties of SERCA mutant E309Q. Glu(309) contributes to Ca(2+) coordination at site II, and a consensus has been that E309Q only binds Ca(2… CONTINUE READING