8SQL

Cleaved Ycf1p Monomer in the Beta Conformation

8SQL の概要

• エントリーDOI: 10.2210/pdb8sql/pdb
• EMDBエントリー: 40709
• 分子名称: Metal resistance protein YCF1, Unknown peptide from Ycf1p R region, PHOSPHATIDYLETHANOLAMINE (3 entities in total)
• 機能のキーワード: abc transporter, transport protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 176616.60

構造登録者

Bickers, S.C.,Benlekbir, S.,Rubinstein, J.L.,Kanelis, V. (登録日: 2023-05-04, 公開日: 2024-05-08, 最終更新日: 2025-05-21)

主引用文献

Bickers, S.C.,Benlekbir, S.,Rubinstein, J.L.,Kanelis, V.
Structure of a dimeric full-length ABC transporter.
Nat Commun, 15:9946-9946, 2024

PubMed Abstract: Activities of ATP binding cassette (ABC) proteins are regulated by multiple mechanisms, including protein interactions, phosphorylation, proteolytic processing, and/or oligomerization of the ABC protein itself. Here we present the structure of yeast cadmium factor 1 (Ycf1p) in its mature form following cleavage by Pep4p protease. Ycf1p, a C subfamily ABC protein (ABCC), is homologue of human multidrug resistance protein 1. Remarkably, a portion of cleaved Ycf1p forms a well-ordered dimer, alongside monomeric particles also present in solution. While numerous other ABC proteins have been proposed to dimerize, no high-resolution structures have been reported. Both phosphorylation of the regulatory (R) region and ATPase activity are lower in the Ycf1p dimer compared to the monomer, indicating that dimerization affects Ycf1p function. The interface between Ycf1p protomers features protein-protein interactions and contains bound lipids, suggesting that lipids stabilize the dimer. The Ycf1p dimer structure may inform the dimerization interfaces of other ABCC dimers.

PubMed: 39550367
DOI: 10.1038/s41467-024-54147-8

実験手法

ELECTRON MICROSCOPY (3.1 Å)