Secondary structure of the Neurospora crassa plasma membrane H+-ATPase as estimated by circular dichroism.

@article{Hennessey1988SecondarySO,
  title={Secondary structure of the Neurospora crassa plasma membrane H+-ATPase as estimated by circular dichroism.},
  author={John P. Hennessey and Gene A. Scarborough},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 7},
  pages={
          3123-30
        }
}
Probing the structure of the Neurospora crassa plasma membrane H+-ATPase
TLDR
A first-generation model for the tertiary structure of the H-ATPase based on information established the topographical location of virtually all of the 919 residues in the H+- ATPase molecule, allowing the formulation of a reasonably detailed model.
The Oligomeric State of the Plasma Membrane H+-ATPase from Kluyveromyces lactis
TLDR
It is concluded that the quaternary structure of the H+-ATPase is the Hexamer and that a relationship seems to exist between ATPase function and the aggregation state of the hexamer.
Crystallization, structure and dynamics of the proton-translocating P-type ATPase.
TLDR
Electron crystallographic analysis of the two-dimensional crystals grown on carbon films has recently elucidated the structure of the H(+) P-ATPase, and results of hydrogen/deuterium exchange experiments indicate that these conformational changes are probably rigid-body interdomain movements that lead to cleft closure.
Emerging Structure of the Neurospora Plasma Membrane H+‐ATPase
The primary goal of this laboratory is to understand the molecular mechanism of membrane transport catalyzed by the proton-translocating ATPase from the plasma membrane of Neurospora crassa, which is
Contribution of infrared spectroscopy to the understanding of the structure of the Neurospora crassa plasma membrane H+-ATPase
TLDR
Among the E1-E2 ATPases, the Neurospora crassa plasma membrane H+-ATPase is well characterised and was shown to be active as a monomer when purified and inserted into a lipid membrane.
Fourier Transform Infrared Spectroscopy Study of the Secondary Structure of the Reconstituted Neurospora crassa Plasma Membrane H-ATPase and of Its Membrane-associated Proteolytic Peptides (*)
TLDR
Amide hydrogen/deuterium exchange kinetics performed for the intact H-ATPase and for the membrane-associated domain demonstrate that this part of ATPase shows less accessibility to the solvent than the entire protein but remains much more accessible to thesolvent than bacteriorhodopsin membrane segments.
Structure, Mechanism, and Regulation of the Neurospora Plasma Membrane H+-ATPase
TLDR
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 reveals the likely path of theproton through the membrane and shows that the nucleotide-binding domain rotates by ∼70° to deliver adenosine triphosphate to the phosphorylation site.
Molecular Mechanism of the P-Type ATPases
TLDR
A nearly complete understanding of the P-type ATPase reaction mechanism is at hand, although a few details await elucidation.
...
...