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Crystal structure of the plasma membrane proton pump
The first structure of a P-type proton pump determined by X-ray crystallography is presented, and the structure is locked in a functional state not previously observed in P- type ATPases.
The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm
The structure of rabbit SERCA1a suggests a mechanism for selective Ca2+ loading and activation of SERCA, and provides new insight into how SLN and PLB inhibition arises from stabilization of this E1 intermediate state without bound Ca2+.
A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps
Structural information provides insight into the function of these two distinct but related P-type pumps, which maintain a proton gradient in plants and fungi and a Na+ and K+ gradient in animal cells.
P-type ATPases as drug targets: tools for medicine and science.
A Novel Mechanism of P-type ATPase Autoinhibition Involving Both Termini of the Protein
- K. Ekberg, M. Palmgren, B. Veierskov, M. Buch-Pedersen
- BiologyThe Journal of Biological Chemistry
- 12 January 2010
It is demonstrated that both the N and the C termini of the plant plasma membrane H+-ATPase are directly involved in controlling the pump activity state and that N-terminal displacements are coupled to secondary modifications taking place at the C- terminal end.
Large-scale purification of the proton pumping pyrophosphatase from Thermotoga maritima: a "Hot-Solve" method for isolation of recombinant thermophilic membrane proteins.
Intracellular Targeting Signals and Lipid Specificity Determinants of the ALA/ALIS P4-ATPase Complex Reside in the Catalytic ALA α-Subunit
- R. López-Marqués, L. R. Poulsen, M. Palmgren
- Biology, ChemistryMolecular biology of the cell
- 1 March 2010
It is demonstrated that cellular targeting and lipid specificity of P4-ATPases require the α- subunit but are independent of the β-subunit, which indicates that the flippase machinery is composed of two pieces.
Protons and how they are transported by proton pumps
- M. Buch-Pedersen, B. P. Pedersen, B. Veierskov, P. Nissen, M. Palmgren
- BiologyPflügers Archiv - European Journal of Physiology
Taking the biochemical and structural data together, the basic molecular components that allow the plasma membrane proton H+-ATPase to carry out proton transport against large membrane potentials are described.
Conserved Asp684 in Transmembrane Segment M6 of the Plant Plasma Membrane P-type Proton Pump AHA2 Is a Molecular Determinant of Proton Translocation*
The finding that the carboxylate side chain of Asp684 contributes to the proton-binding site and appears to function as an absolutely essential proton acceptor along the propton transport pathway is discussed in the context of a possible proton pumping mechanism of P-type H+-ATPases.
Potassium as an Intrinsic Uncoupler of the Plasma Membrane H+-ATPase*
- M. Buch-Pedersen, E. Rudashevskaya, T. Berner, K. Venema, M. Palmgren
- BiologyJournal of Biological Chemistry
- 15 December 2006
K+ is identified as an intrinsic uncoupler of the proton pump and a mechanism for control of the H+/ATP coupling ratio is suggested, which may serve regulatory purposes and play a role in negative regulation of the transmembrane electrochemical gradient under cellular conditions where E1P is accumulating.