4YTX

Crystal structure of Ups1-Mdm35 complex with PA

4YTX の概要

• エントリーDOI: 10.2210/pdb4ytx/pdb
• 関連するPDBエントリー: 4YTV 4YTW
• 分子名称: Mitochondrial distribution and morphology protein 35, Protein UPS1, mitochondrial, 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE (3 entities in total)
• 機能のキーワード: phospholipid transfer, mitochondria, phosphatidic acid, lipid transport
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 242945.08

構造登録者

Watanabe, Y.,Tamura, Y.,Kawano, S.,Endo, T. (登録日: 2015-03-18, 公開日: 2015-08-12, 最終更新日: 2024-11-06)

主引用文献

Watanabe, Y.,Tamura, Y.,Kawano, S.,Endo, T.
Structural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria.
Nat Commun, 6:7922-7922, 2015

PubMed Abstract: Eukaryotic cells are compartmentalized into membrane-bounded organelles whose functions rely on lipid trafficking to achieve membrane-specific compositions of lipids. Here we focused on the Ups1-Mdm35 system, which mediates phosphatidic acid (PA) transfer between the outer and inner mitochondrial membranes, and determined the X-ray structures of Mdm35 and Ups1-Mdm35 with and without PA. The Ups1-Mdm35 complex constitutes a single domain that has a deep pocket and flexible Ω-loop lid. Structure-based mutational analyses revealed that a basic residue at the pocket bottom and the Ω-loop lid are important for PA extraction from the membrane following Ups1 binding. Ups1 binding to the membrane is enhanced by the dissociation of Mdm35. We also show that basic residues around the pocket entrance are important for Ups1 binding to the membrane and PA extraction. These results provide a structural basis for understanding the mechanism of PA transfer between mitochondrial membranes.

PubMed: 26235513
DOI: 10.1038/ncomms8922

実験手法

X-RAY DIFFRACTION (3.2 Å)