Publication

pH- and sodium-induced changes in a sodium/proton antiporter

Batista Paulino, C. & Kuehlbrandt, W., 28-Jan-2014, In : eLife. 3, p. 1-13 13 p., e01412.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Batista Paulino, C., & Kuehlbrandt, W. (2014). pH- and sodium-induced changes in a sodium/proton antiporter. eLife, 3, 1-13. [e01412]. https://doi.org/10.7554/eLife.01412

Author

Batista Paulino, Cristina ; Kuehlbrandt, Werner. / pH- and sodium-induced changes in a sodium/proton antiporter. In: eLife. 2014 ; Vol. 3. pp. 1-13.

Harvard

Batista Paulino, C & Kuehlbrandt, W 2014, 'pH- and sodium-induced changes in a sodium/proton antiporter' eLife, vol. 3, e01412, pp. 1-13. https://doi.org/10.7554/eLife.01412

Standard

pH- and sodium-induced changes in a sodium/proton antiporter. / Batista Paulino, Cristina; Kuehlbrandt, Werner.

In: eLife, Vol. 3, e01412, 28.01.2014, p. 1-13.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Batista Paulino C, Kuehlbrandt W. pH- and sodium-induced changes in a sodium/proton antiporter. eLife. 2014 Jan 28;3:1-13. e01412. https://doi.org/10.7554/eLife.01412


BibTeX

@article{e9ca8fdbc7e94e41adba535f37e2e893,
title = "pH- and sodium-induced changes in a sodium/proton antiporter",
abstract = "We examined substrate-induced conformational changes in MjNhaP1, an archaeal electroneutral Na+/H+-antiporter resembling the human antiporter NHE1, by electron crystallography of 2D crystals in a range of physiological pH and Na+ conditions. In the absence of sodium, changes in pH had no major effect. By contrast, changes in Na+ concentration caused a marked conformational change that was largely pH-independent. Crystallographically determined, apparent dissociation constants indicated similar to 10-fold stronger Na+ binding at pH 8 than at pH 4, consistent with substrate competition for a common ion-binding site. Projection difference maps indicated helix movements by about 2 angstrom in the 6-helix bundle region of MjNhaP1 that is thought to contain the ion translocation site. We propose that these movements convert the antiporter from the proton-bound, outward-open state to the Na+-bound, inward-open state. Oscillation between the two states would result in rapid Na+/H+ antiport.",
keywords = "sodium/proton antiporter, pH, sodium, cryo-EM",
author = "{Batista Paulino}, Cristina and Werner Kuehlbrandt",
year = "2014",
month = "1",
day = "28",
doi = "10.7554/eLife.01412",
language = "English",
volume = "3",
pages = "1--13",
journal = "eLife",
issn = "2050-084X",
publisher = "ELIFE SCIENCES PUBLICATIONS LTD",

}

RIS

TY - JOUR

T1 - pH- and sodium-induced changes in a sodium/proton antiporter

AU - Batista Paulino, Cristina

AU - Kuehlbrandt, Werner

PY - 2014/1/28

Y1 - 2014/1/28

N2 - We examined substrate-induced conformational changes in MjNhaP1, an archaeal electroneutral Na+/H+-antiporter resembling the human antiporter NHE1, by electron crystallography of 2D crystals in a range of physiological pH and Na+ conditions. In the absence of sodium, changes in pH had no major effect. By contrast, changes in Na+ concentration caused a marked conformational change that was largely pH-independent. Crystallographically determined, apparent dissociation constants indicated similar to 10-fold stronger Na+ binding at pH 8 than at pH 4, consistent with substrate competition for a common ion-binding site. Projection difference maps indicated helix movements by about 2 angstrom in the 6-helix bundle region of MjNhaP1 that is thought to contain the ion translocation site. We propose that these movements convert the antiporter from the proton-bound, outward-open state to the Na+-bound, inward-open state. Oscillation between the two states would result in rapid Na+/H+ antiport.

AB - We examined substrate-induced conformational changes in MjNhaP1, an archaeal electroneutral Na+/H+-antiporter resembling the human antiporter NHE1, by electron crystallography of 2D crystals in a range of physiological pH and Na+ conditions. In the absence of sodium, changes in pH had no major effect. By contrast, changes in Na+ concentration caused a marked conformational change that was largely pH-independent. Crystallographically determined, apparent dissociation constants indicated similar to 10-fold stronger Na+ binding at pH 8 than at pH 4, consistent with substrate competition for a common ion-binding site. Projection difference maps indicated helix movements by about 2 angstrom in the 6-helix bundle region of MjNhaP1 that is thought to contain the ion translocation site. We propose that these movements convert the antiporter from the proton-bound, outward-open state to the Na+-bound, inward-open state. Oscillation between the two states would result in rapid Na+/H+ antiport.

KW - sodium/proton antiporter

KW - pH

KW - sodium

KW - cryo-EM

U2 - 10.7554/eLife.01412

DO - 10.7554/eLife.01412

M3 - Article

VL - 3

SP - 1

EP - 13

JO - eLife

JF - eLife

SN - 2050-084X

M1 - e01412

ER -

ID: 54073264