7QKS

Cryo-EM structure of ABC transporter STE6-2p from Pichia pastoris in apo conformation at 3.1 A resolution

7QKS の概要

• エントリーDOI: 10.2210/pdb7qks/pdb
• 関連するPDBエントリー: 7QKR
• EMDBエントリー: 14050
• 分子名称: Plasma membrane ATP-binding cassette transporter required for the export of a-factor, (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en (2 entities in total)
• 機能のキーワード: abc transporter, abcb, mdr, membrane protein, pichia pastoris, transport protein
• 由来する生物種: Komagataella phaffii CBS 7435
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 145519.07

構造登録者

Schleker, E.S.M.,Reinhart, C. (登録日: 2021-12-18, 公開日: 2022-10-26, 最終更新日: 2024-07-17)

主引用文献

Schleker, E.S.M.,Buschmann, S.,Xie, H.,Welsch, S.,Michel, H.,Reinhart, C.
Structural and functional investigation of ABC transporter STE6-2p from Pichia pastoris reveals unexpected interaction with sterol molecules.
Proc.Natl.Acad.Sci.USA, 119:e2202822119-e2202822119, 2022

PubMed Abstract: Adenosine triphosphate (ATP)-binding cassette (ABC) transporters are multidomain transmembrane proteins, which facilitate the transport of various substances across cell membranes using energy derived from ATP hydrolysis. They are important drug targets since they mediate decreased drug susceptibility during pharmacological treatments. For the methylotrophic yeast , a model organism that is a widely used host for protein expression, the role and function of its ABC transporters is unexplored. In this work, we investigated the ABC-B transporter STE6-2p. Functional investigations revealed that STE6-2p is capable of transporting rhodamines in vivo and is active in the presence of verapamil and triazoles in vitro. A phylogenetic analysis displays homology among multidrug resistance (MDR) transporters from pathogenic fungi to human ABC-B transporters. Further, we present high-resolution single-particle electron cryomicroscopy structures of an ABC transporter from in the apo conformation (3.1 Å) and in complex with verapamil and adenylyl imidodiphosphate (AMP-PNP) (3.2 Å). An unknown density between transmembrane helices 4, 5, and 6 in both structures suggests the presence of a sterol-binding site of unknown function.

PubMed: 36256814
DOI: 10.1073/pnas.2202822119

実験手法

ELECTRON MICROSCOPY (3.1 Å)