5NC8

Shewanella denitrificans Kef CTD in AMP bound form

5NC8 の概要

• エントリーDOI: 10.2210/pdb5nc8/pdb
• 分子名称: Potassium efflux system protein, ADENOSINE MONOPHOSPHATE (2 entities in total)
• 機能のキーワード: ktn/rck domain, kef, amp, potassium efflux, transport protein
• 由来する生物種: Shewanella denitrificans OS217
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53584.00

構造登録者

Pliotas, C.,Naismith, J.H. (登録日: 2017-03-03, 公開日: 2017-04-12, 最終更新日: 2024-01-17)

主引用文献

Pliotas, C.,Grayer, S.C.,Ekkerman, S.,Chan, A.K.N.,Healy, J.,Marius, P.,Bartlett, W.,Khan, A.,Cortopassi, W.A.,Chandler, S.A.,Rasmussen, T.,Benesch, J.L.P.,Paton, R.S.,Claridge, T.D.W.,Miller, S.,Booth, I.R.,Naismith, J.H.,Conway, S.J.
Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificans Kef Potassium Efflux System.
Biochemistry, 56:4219-4234, 2017

PubMed 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.

PubMed: 28656748
DOI: 10.1021/acs.biochem.7b00300

実験手法

X-RAY DIFFRACTION (3.09 Å)