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

Maike Bublitz; Hanne Poulsen; Jens Preben Morth; Poul Nissen

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

Maike Bublitz, Hanne Poulsen, Jens Preben Morth, Poul Nissen

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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.

Original language	English
Journal	Current Opinion in Structural Biology
Volume	20
Issue	4
Pages (from-to)	431-439.
ISSN	0959-440X
Publication status	Published - 2010

Cite this

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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",

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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

SN - 0959-440X

VL - 20

SP - 431-439.

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 4

ER -