7M69

E1435Q Ycf1 mutant in inward-facing wide conformation

7M69 の概要

• エントリーDOI: 10.2210/pdb7m69/pdb
• EMDBエントリー: 23691
• 分子名称: Metal resistance protein YCF1 (1 entity in total)
• 機能のキーワード: abc transporter, membrane protein
• 由来する生物種: Saccharomyces cerevisiae S288C
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 176318.33

構造登録者

Khandelwal, N.K.,Millan, C.R.,Thaker, T.M.,Tomasiak, T.M. (登録日: 2021-03-25, 公開日: 2022-04-06, 最終更新日: 2024-10-16)

主引用文献

Khandelwal, N.K.,Millan, C.R.,Zangari, S.I.,Avila, S.,Williams, D.,Thaker, T.M.,Tomasiak, T.M.
The structural basis for regulation of the glutathione transporter Ycf1 by regulatory domain phosphorylation.
Nat Commun, 13:1278-1278, 2022

PubMed Abstract: Yeast Cadmium Factor 1 (Ycf1) sequesters heavy metals and glutathione into the vacuole to counter cell stress. Ycf1 belongs to the ATP binding cassette C-subfamily (ABCC) of transporters, many of which are regulated by phosphorylation on intrinsically-disordered domains. The regulatory mechanism of phosphorylation is still poorly understood. Here, we report two cryo-EM structures of Ycf1 at 3.4 Å and 4.0 Å resolution in inward-facing open conformations that capture previously unobserved ordered states of the intrinsically disordered regulatory domain (R-domain). R-domain phosphorylation is clearly evident and induces a topology promoting electrostatic and hydrophobic interactions with Nucleotide Binding Domain 1 (NBD1) and the Lasso motif. These interactions stay constant between the structures and are related by rigid body movements of the NBD1/R-domain complex. Biochemical data further show R-domain phosphorylation reorganizes the Ycf1 architecture and is required for maximal ATPase activity. Together, we provide insights into how R-domains control ABCC transporter activity.

PubMed: 35277487
DOI: 10.1038/s41467-022-28811-w

実験手法

ELECTRON MICROSCOPY (3.42 Å)