Aarhus University Seal / Aarhus Universitets segl

English

Du er her: AU » Om AU » Organisation » In and out of the cation pumps: P-type ATPase structure r...

Om AU

In and out of the cation pumps: P-type ATPase structure revisited.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Standard

In and out of the cation pumps: P-type ATPase structure revisited. / Bublitz, Maike; Poulsen, Hanne; Morth, Jens Preben; Nissen, Poul.

I: Current Opinion in Structural Biology, Bind 20, Nr. 4, 2010, s. 431-439.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Bublitz, M, Poulsen, H, Morth, JP & Nissen, P 2010, 'In and out of the cation pumps: P-type ATPase structure revisited.', Current Opinion in Structural Biology, bind 20, nr. 4, s. 431-439..

APA

Bublitz, M., Poulsen, H., Morth, J. P., & Nissen, P. (2010). In and out of the cation pumps: P-type ATPase structure revisited. Current Opinion in Structural Biology, 20(4), 431-439..

CBE

Bublitz M, Poulsen H, Morth JP, Nissen P. 2010. In and out of the cation pumps: P-type ATPase structure revisited. Current Opinion in Structural Biology. 20(4):431-439.

MLA

Bublitz, Maike o.a.. "In and out of the cation pumps: P-type ATPase structure revisited.". Current Opinion in Structural Biology. 2010, 20(4). 431-439.

Vancouver

Bublitz M, Poulsen H, Morth JP, Nissen P. In and out of the cation pumps: P-type ATPase structure revisited. Current Opinion in Structural Biology. 2010;20(4):431-439.

Author

Bublitz, Maike ; Poulsen, Hanne ; Morth, Jens Preben ; Nissen, Poul. / In and out of the cation pumps: P-type ATPase structure revisited. I: Current Opinion in Structural Biology. 2010 ; Bind 20, Nr. 4. s. 431-439.

Bibtex

@article{41155a9017c04be49748f4161afba3ff,
title = "In and out of the cation pumps: P-type ATPase structure revisited.",
abstract = "Active transport across membranes is a crucial requirement for life. P-type ATPases build up electrochemical gradients at the expense of ATP by forming and splitting a covalent phosphoenzyme intermediate, coupled to conformational changes in the transmembrane section where the ions are translocated. The marked increment during the last three years in the number of crystal structures of P-type ATPases has greatly improved our understanding of the similarities and differences of pumps with different ion specificities, since the structures of the Ca2+-ATPase, the Na+,K+-ATPase and the H+-ATPase can now be compared directly. Mechanisms for ion gating, charge neutralization and backflow prevention are starting to emerge from comparative structural analysis; and in combination with functional studies of mutated pumps this provides a framework for speculating on how the ions are bound and released as well as on how specificity is achieved.",
author = "Maike Bublitz and Hanne Poulsen and Morth, {Jens Preben} and Poul Nissen",
year = "2010",
language = "English",
volume = "20",
pages = "431--439.",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Ltd. * Current Opinion Journals",
number = "4",

}

RIS

TY - JOUR

T1 - In and out of the cation pumps: P-type ATPase structure revisited.

AU - Bublitz, Maike

AU - Poulsen, Hanne

AU - Morth, Jens Preben

AU - Nissen, Poul

PY - 2010

Y1 - 2010

N2 - Active transport across membranes is a crucial requirement for life. P-type ATPases build up electrochemical gradients at the expense of ATP by forming and splitting a covalent phosphoenzyme intermediate, coupled to conformational changes in the transmembrane section where the ions are translocated. The marked increment during the last three years in the number of crystal structures of P-type ATPases has greatly improved our understanding of the similarities and differences of pumps with different ion specificities, since the structures of the Ca2+-ATPase, the Na+,K+-ATPase and the H+-ATPase can now be compared directly. Mechanisms for ion gating, charge neutralization and backflow prevention are starting to emerge from comparative structural analysis; and in combination with functional studies of mutated pumps this provides a framework for speculating on how the ions are bound and released as well as on how specificity is achieved.

AB - Active transport across membranes is a crucial requirement for life. P-type ATPases build up electrochemical gradients at the expense of ATP by forming and splitting a covalent phosphoenzyme intermediate, coupled to conformational changes in the transmembrane section where the ions are translocated. The marked increment during the last three years in the number of crystal structures of P-type ATPases has greatly improved our understanding of the similarities and differences of pumps with different ion specificities, since the structures of the Ca2+-ATPase, the Na+,K+-ATPase and the H+-ATPase can now be compared directly. Mechanisms for ion gating, charge neutralization and backflow prevention are starting to emerge from comparative structural analysis; and in combination with functional studies of mutated pumps this provides a framework for speculating on how the ions are bound and released as well as on how specificity is achieved.

M3 - Journal article

VL - 20

SP - 431-439.

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

IS - 4

ER -