Polarity of the ATP binding site of the Na<sup>+</sup>,K<sup>+</sup>-ATPase, gastric H<sup>+</sup>,K<sup>+</sup>-ATPase and sarcoplasmic reticulum Ca<sup>2+</sup>-ATPase.
- Publisher:
- ELSEVIER
- Publication Type:
- Journal Article
- Citation:
- Biochimica et biophysica acta. Biomembranes, 2020, 1862, (2)
- Issue Date:
- 2020-02
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1-s2.0-S000527361930286X-main.pdf | 1.2 MB | Adobe PDF |
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Hossain, KR | |
dc.contributor.author | Li, X | |
dc.contributor.author | Zhang, T | |
dc.contributor.author | Paula, S | |
dc.contributor.author | Cornelius, F | |
dc.contributor.author | Clarke, RJ | |
dc.date.accessioned | 2021-03-17T00:34:31Z | |
dc.date.available | 2019-11-27 | |
dc.date.available | 2021-03-17T00:34:31Z | |
dc.date.issued | 2020-02 | |
dc.identifier.citation | Biochimica et biophysica acta. Biomembranes, 2020, 1862, (2) | |
dc.identifier.issn | 0005-2736 | |
dc.identifier.issn | 1879-2642 | |
dc.identifier.uri | http://hdl.handle.net/10453/147280 | |
dc.description.abstract | A fluorescence ratiometric method utilizing the probe eosin Y is presented for estimating the ATP binding site polarity of P-type ATPases in different conformational states. The method has been calibrated by measurements in a series of alcohols and tested using complexation of eosin Y with methyl-β-cyclodextrin. The results obtained with the Na<sup>+</sup>,K<sup>+</sup>-, H<sup>+</sup>,K<sup>+</sup>- and sarcoplasmic reticulum Ca<sup>2+</sup>-ATPases indicate that the ATP binding site, to which eosin is known to bind, is significantly more polar in the case of the Na<sup>+</sup>,K<sup>+</sup>- and H<sup>+</sup>,K<sup>+</sup>-ATPases compared to the Ca<sup>2+</sup>-ATPase. This result was found to be consistent with docking calculations of eosin with the E2 conformational state of the Na<sup>+</sup>,K<sup>+</sup>-ATPase and the Ca<sup>2+</sup>-ATPase. Fluorescence experiments showed that eosin binds significantly more strongly to the E1 conformation of the Na<sup>+</sup>,K<sup>+</sup>-ATPase than the E2 conformation, but in the case of the Ca<sup>2+</sup>-ATPase both fluorescence experiments and docking calculations showed no significant difference in binding affinity between the two conformations. This result could be due to the fact that, in contrast to the Na<sup>+</sup>,K<sup>+</sup>- and H<sup>+</sup>,K<sup>+</sup>-ATPases, the E2-E1 transition of the Ca<sup>2+</sup>-ATPase does not involve the movement of a lysine-rich N-terminal tail which may affect the overall enzyme conformation. Consistent with this hypothesis, the eosin affinity of the E1 conformation of the Na<sup>+</sup>,K<sup>+</sup>-ATPase was significantly reduced after N-terminal truncation. It is suggested that changes in conformational entropy of the N-terminal tail of the Na<sup>+</sup>, K<sup>+</sup>- and the H<sup>+</sup>,K<sup>+</sup>-ATPases during the E2-E1 transition could affect the thermodynamic stability of the E1 conformation and hence its ATP binding affinity. | |
dc.format | Print-Electronic | |
dc.language | eng | |
dc.publisher | ELSEVIER | |
dc.relation.ispartof | Biochimica et biophysica acta. Biomembranes | |
dc.relation.isbasedon | 10.1016/j.bbamem.2019.183138 | |
dc.rights | info:eu-repo/semantics/closedAccess | |
dc.subject | 0601 Biochemistry and Cell Biology, 0699 Other Biological Sciences, 0904 Chemical Engineering | |
dc.subject.classification | Biophysics | |
dc.subject.classification | Biochemistry & Molecular Biology | |
dc.subject.mesh | Adenosine Triphosphate | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Binding Sites | |
dc.subject.mesh | Gastric Mucosa | |
dc.subject.mesh | Molecular Docking Simulation | |
dc.subject.mesh | Protein Binding | |
dc.subject.mesh | Sarcoplasmic Reticulum Calcium-Transporting ATPases | |
dc.subject.mesh | Sodium-Potassium-Exchanging ATPase | |
dc.subject.mesh | Swine | |
dc.subject.mesh | Gastric Mucosa | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Swine | |
dc.subject.mesh | Adenosine Triphosphate | |
dc.subject.mesh | Binding Sites | |
dc.subject.mesh | Protein Binding | |
dc.subject.mesh | Sarcoplasmic Reticulum Calcium-Transporting ATPases | |
dc.subject.mesh | Sodium-Potassium-Exchanging ATPase | |
dc.subject.mesh | Molecular Docking Simulation | |
dc.subject.mesh | Adenosine Triphosphate | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Binding Sites | |
dc.subject.mesh | Gastric Mucosa | |
dc.subject.mesh | Molecular Docking Simulation | |
dc.subject.mesh | Protein Binding | |
dc.subject.mesh | Sarcoplasmic Reticulum Calcium-Transporting ATPases | |
dc.subject.mesh | Sodium-Potassium-Exchanging ATPase | |
dc.subject.mesh | Swine | |
dc.title | Polarity of the ATP binding site of the Na<sup>+</sup>,K<sup>+</sup>-ATPase, gastric H<sup>+</sup>,K<sup>+</sup>-ATPase and sarcoplasmic reticulum Ca<sup>2+</sup>-ATPase. | |
dc.type | Journal Article | |
utslib.citation.volume | 1862 | |
utslib.location.activity | Netherlands | |
utslib.for | 0601 Biochemistry and Cell Biology | |
utslib.for | 0699 Other Biological Sciences | |
utslib.for | 0904 Chemical Engineering | |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
utslib.copyright.status | closed_access | * |
pubs.consider-herdc | false | |
dc.date.updated | 2021-03-17T00:34:29Z | |
pubs.issue | 2 | |
pubs.publication-status | Published | |
pubs.volume | 1862 | |
utslib.citation.issue | 2 |
Abstract:
A fluorescence ratiometric method utilizing the probe eosin Y is presented for estimating the ATP binding site polarity of P-type ATPases in different conformational states. The method has been calibrated by measurements in a series of alcohols and tested using complexation of eosin Y with methyl-β-cyclodextrin. The results obtained with the Na+,K+-, H+,K+- and sarcoplasmic reticulum Ca2+-ATPases indicate that the ATP binding site, to which eosin is known to bind, is significantly more polar in the case of the Na+,K+- and H+,K+-ATPases compared to the Ca2+-ATPase. This result was found to be consistent with docking calculations of eosin with the E2 conformational state of the Na+,K+-ATPase and the Ca2+-ATPase. Fluorescence experiments showed that eosin binds significantly more strongly to the E1 conformation of the Na+,K+-ATPase than the E2 conformation, but in the case of the Ca2+-ATPase both fluorescence experiments and docking calculations showed no significant difference in binding affinity between the two conformations. This result could be due to the fact that, in contrast to the Na+,K+- and H+,K+-ATPases, the E2-E1 transition of the Ca2+-ATPase does not involve the movement of a lysine-rich N-terminal tail which may affect the overall enzyme conformation. Consistent with this hypothesis, the eosin affinity of the E1 conformation of the Na+,K+-ATPase was significantly reduced after N-terminal truncation. It is suggested that changes in conformational entropy of the N-terminal tail of the Na+, K+- and the H+,K+-ATPases during the E2-E1 transition could affect the thermodynamic stability of the E1 conformation and hence its ATP binding affinity.
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