Adenosine monophosphate binding stabilizes the KTN domain of the Shewanella denitrificans Kef potassium efflux system
Abstract: Ligand binding is one of the most fundamental properties of proteins. Ligand functions fall into three basic types: substrates, regulatory molecules, and cofactors essential to protein stability, reactivity, or enzyme–substrate complex formation. The regulation of potassium ion movement in bacteria is predominantly under the control of regulatory ligands that gate the relevant channels and transporters, which possess subunits or domains that contain Rossmann folds (RFs). Here we demonstrate that adenosine monophosphate (AMP) is bound to both RFs of the dimeric bacterial Kef potassium efflux system (Kef), where it plays a structural role. We conclude that AMP binds with high affinity, ensuring that the site is fully occupied at all times in the cell. Loss of the ability to bind AMP, we demonstrate, causes protein, and likely dimer, instability and consequent loss of function. Kef system function is regulated via the reversible binding of comparatively low-affinity glutathione-based ligands at the interface between the dimer subunits. We propose this interfacial binding site is itself stabilized, at least in part, by AMP binding
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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Biochemistry. - 56, 32 (2017) , 4219-4234, ISSN: 0006-2960
- Event
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Veröffentlichung
- (where)
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Freiburg
- (who)
-
Universität
- (when)
-
2019
- Creator
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Pliotas, Christos
Grayer, Samuel C.
Ekkerman, Silvia
Chan, Anthony K. N.
Healy, Jess
Marius, Phedra
Bartlett, Wendy
Khan, Amjad
Cortopassi, Wilian A.
Chandler, Shane A.
Rasmussen, Tim
Benesch, Justin L. P.
Paton, Robert S.
Claridge, Timothy D. W.
Miller, Samantha
Booth, Ian R.
Naismith, James H.
Conway, Stuart J.
- DOI
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10.1021/acs.biochem.7b00300
- URN
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urn:nbn:de:bsz:25-freidok-1438757
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:52 PM CET
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Pliotas, Christos
- Grayer, Samuel C.
- Ekkerman, Silvia
- Chan, Anthony K. N.
- Healy, Jess
- Marius, Phedra
- Bartlett, Wendy
- Khan, Amjad
- Cortopassi, Wilian A.
- Chandler, Shane A.
- Rasmussen, Tim
- Benesch, Justin L. P.
- Paton, Robert S.
- Claridge, Timothy D. W.
- Miller, Samantha
- Booth, Ian R.
- Naismith, James H.
- Conway, Stuart J.
- Universität
Time of origin
- 2019
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Adenosine receptors and singnaling in the kidney
Irreversible Antagonists for the Adenosine A2B Receptor
The glycoprotein nature of A1 adenosine receptors
Ktn
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The putative drug efflux systems of the Bacillus cereus group
The effect of high extracellular potassium on the kinetics of potassium conductance of the squid axon membrane
Mathematical models for the quantification of the metabolism of adenosine
Probing the Local Environment in Potassium Salts and Potassium-Promoted Catalysts by Potassium Valence-to-Core X-ray Emission Spectroscopy
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Adenosine receptors and singnaling in the kidney
Irreversible Antagonists for the Adenosine A2B Receptor
The glycoprotein nature of A1 adenosine receptors
Ktn
Ktn
The putative drug efflux systems of the Bacillus cereus group
The effect of high extracellular potassium on the kinetics of potassium conductance of the squid axon membrane
Mathematical models for the quantification of the metabolism of adenosine
Probing the Local Environment in Potassium Salts and Potassium-Promoted Catalysts by Potassium Valence-to-Core X-ray Emission Spectroscopy
Adenosine: receptors and modulation of cell function ; proceedings of the International Workshop on Adenosine and Xanthine Derivatives