7LC3

CryoEM Structure of KdpFABC in E1-ATP state

7LC3 の概要

• エントリーDOI: 10.2210/pdb7lc3/pdb
• EMDBエントリー: 23268
• 分子名称: Potassium-transporting ATPase potassium-binding subunit, Potassium-transporting ATPase ATP-binding subunit, Potassium-transporting ATPase KdpC subunit, ... (9 entities in total)
• 機能のキーワード: p-type atpase, atp-dependent potassium pump, membrane protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 158196.20

構造登録者

Sweet, M.E.,Larsen, C.,Pedersen, B.P.,Stokes, D.L. (登録日: 2021-01-09, 公開日: 2021-01-27, 最終更新日: 2024-05-29)

主引用文献

Sweet, M.E.,Larsen, C.,Zhang, X.,Schlame, M.,Pedersen, B.P.,Stokes, D.L.
Structural basis for potassium transport in prokaryotes by KdpFABC.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: KdpFABC is an oligomeric K transport complex in prokaryotes that maintains ionic homeostasis under stress conditions. The complex comprises a channel-like subunit (KdpA) from the superfamily of K transporters and a pump-like subunit (KdpB) from the superfamily of P-type ATPases. Recent structural work has defined the architecture and generated contradictory hypotheses for the transport mechanism. Here, we use substrate analogs to stabilize four key intermediates in the reaction cycle and determine the corresponding structures by cryogenic electron microscopy. We find that KdpB undergoes conformational changes consistent with other representatives from the P-type superfamily, whereas KdpA, KdpC, and KdpF remain static. We observe a series of spherical densities that we assign as K or water and which define a pathway for K transport. This pathway runs through an intramembrane tunnel in KdpA and delivers ions to sites in the membrane domain of KdpB. Our structures suggest a mechanism where ATP hydrolysis is coupled to K transfer between alternative sites in KdpB, ultimately reaching a low-affinity site where a water-filled pathway allows release of K to the cytoplasm.

PubMed: 34272288
DOI: 10.1073/pnas.2105195118

実験手法

ELECTRON MICROSCOPY (3.23 Å)