Structure, Mechanism, and Regulation of the Neurospora Plasma Membrane H+-ATPase

@article{Khlbrandt2002StructureMA,
  title={Structure, Mechanism, and Regulation of the Neurospora Plasma Membrane H+-ATPase},
  author={Werner K{\"u}hlbrandt and Johan P. Zeelen and Jens Dietrich},
  journal={Science},
  year={2002},
  volume={297},
  pages={1692 - 1696}
}
Proton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic homology model of the proton pump based on the 2.6 angstrom x-ray structure of the related Ca2+ pump from rabbit sarcoplasmic reticulum. The model, when fitted to an 8 angstrom map of theNeurospora proton pump determined by electron microscopy, reveals the likely path of the proton through the membrane… 
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References

SHOWING 1-10 OF 59 REFERENCES
Three-dimensional map of the plasma membrane H+-ATPase in the open conformation
TLDR
A three-dimensional map of the H+-ATPase is obtained by electron crystallography of two-dimensional crystals grown directly on electron microscope grids and reveals ten membrane-spanning α-helices in the membrane domain, and four major cytoplasmic domains in the open conformation of the enzyme without bound ligands.
Regulation of Yeast H+-ATPase by Protein Kinases Belonging to a Family Dedicated to Activation of Plasma Membrane Transporters
TLDR
Two genes from Saccharomyces cerevisiae are characterized that encode protein kinases implicated in activation of the yeast plasma membrane H+-ATPase (Pma1) in response to glucose metabolism, and ptk2 mutants exhibited reduced uptake of lithium and methylammonium.
Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
TLDR
Comparison with a low-resolution electron density map of the enzyme in the absence of calcium and with biochemical data suggests that large domain movements take place during active transport.
Domain movements of plasma membrane H+‐ATPase: 3D structures of two states by electron cryo‐microscopy
TLDR
Structural comparisons indicate that there is a rearrangement of the cytoplasmic domain on Mg2+/ADP binding, which consists of a movement of mass towards the 6‐fold axis causing the structure to become more compact, accompanied by a modest conformational change in the transmembrane domain.
Structure of the calcium pump from sarcoplasmic reticulum at 8-Å resolution
TLDR
A distinct cavity leads to the putative calcium-binding site, providing a plausible path for calcium release to the lumen of the sarcoplasmic reticulum.
The regulatory domain of fungal and plant plasma membrane H(+)-ATPase.
TLDR
The activity of fungal and plant plasma membrane H(+)-ATPases seems to be regulated by modulation of the interaction of an inhibitory domain at the C-terminus with the active site, and genetic evidence for domain interaction is provided.
A structural model for the catalytic cycle of Ca(2+)-ATPase.
TLDR
It is hypothesized that both the nucleotide-binding and beta-sheet domains are highly mobile and driven by Brownian motion to elicit phosphoenzyme formation and calcium transport, respectively, and the reaction cycle of Ca(2+)-ATPase would have elements of a Brownian ratchet.
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