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AMP binding stabilizes the KTN domain of the Shewanella denitrificans Kef potassium efflux system

Pliotas, C; Grayer, SC; Ekkerman, S; Chan, AKN; Healy, J; Marius, P; Bartlett, W; ... Conway, SJ; + view all (2017) AMP binding stabilizes the KTN domain of the Shewanella denitrificans Kef potassium efflux system. Biochemistry , 56 (32) pp. 4219-4234. 10.1021/acs.biochem.7b00300. Green open access

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Abstract

Ligand binding is one of the most fundamental properties of proteins. Ligand functions fall into three basic types: substrates, regulatory molecules, and co-factors 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 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. Regulation of Kef system function is 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 stabilised, at least in part, by AMP binding.

Type: Article
Title: AMP binding stabilizes the KTN domain of the Shewanella denitrificans Kef potassium efflux system
Open access status: An open access version is available from UCL Discovery
DOI: 10.1021/acs.biochem.7b00300
Publisher version: http://dx.doi.org/10.1021/acs.biochem.7b00300
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy > SoP Pharmaceutical and Bio Chemistry
URI: https://discovery.ucl.ac.uk/id/eprint/1563522
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