Structure and activation mechanism of the hexameric plasma membrane H+-ATPase

@article{Zhao2021StructureAA,
  title={Structure and activation mechanism of the hexameric plasma membrane H+-ATPase},
  author={Peng Zhao and Chaoran Zhao and Dandan Chen and Caihong Yun and Huilin Li and Lin Bai},
  journal={Nature Communications},
  year={2021},
  volume={12}
}
The S. cerevisiae plasma membrane H+-ATPase, Pma1, is a P3A-type ATPase and the primary protein component of the membrane compartment of Pma1 (MCP). Like other plasma membrane H+-ATPases, Pma1 assembles and functions as a hexamer, a property unique to this subfamily among the larger family of P-type ATPases. It has been unclear how Pma1 organizes the yeast membrane into MCP microdomains, or why it is that Pma1 needs to assemble into a hexamer to establish the membrane electrochemical proton… 
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