7NNP

Rb-loaded cryo-EM structure of the E1-ATP KdpFABC complex.

7NNP の概要

• エントリーDOI: 10.2210/pdb7nnp/pdb
• 関連するPDBエントリー: 7NNL
• EMDBエントリー: 12478 12482
• 分子名称: Potassium-transporting ATPase potassium-binding subunit, Potassium-transporting ATPase KdpC subunit, Potassium-transporting ATPase KdpF subunit, ... (7 entities in total)
• 機能のキーワード: p-type atpase, superfamily of k+ transporters (skt), rb substitution, intersubunit tunnel, membrane protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 158780.06

構造登録者

Silberberg, J.M.,Corey, R.A.,Hielkema, L.,Stock, C.,Stansfeld, P.J.,Paulino, C.,Haenelt, I. (登録日: 2021-02-25, 公開日: 2021-07-28, 最終更新日: 2024-07-10)

主引用文献

Silberberg, J.M.,Corey, R.A.,Hielkema, L.,Stock, C.,Stansfeld, P.J.,Paulino, C.,Hanelt, I.
Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC.
Nat Commun, 12:5098-5098, 2021

PubMed Abstract: KdpFABC, a high-affinity K pump, combines the ion channel KdpA and the P-type ATPase KdpB to secure survival at K limitation. Here, we apply a combination of cryo-EM, biochemical assays, and MD simulations to illuminate the mechanisms underlying transport and the coupling to ATP hydrolysis. We show that ions are transported via an intersubunit tunnel through KdpA and KdpB. At the subunit interface, the tunnel is constricted by a phenylalanine, which, by polarized cation-π stacking, controls K entry into the canonical substrate binding site (CBS) of KdpB. Within the CBS, ATPase coupling is mediated by the charge distribution between an aspartate and a lysine. Interestingly, individual elements of the ion translocation mechanism of KdpFABC identified here are conserved among a wide variety of P-type ATPases from different families. This leads us to the hypothesis that KdpB might represent an early descendant of a common ancestor of cation pumps.

PubMed: 34429416
DOI: 10.1038/s41467-021-25242-x

実験手法

ELECTRON MICROSCOPY (3.2 Å)