6E7O

Crystal structure of deglycosylated human EPDR1

6E7O の概要

• エントリーDOI: 10.2210/pdb6e7o/pdb
• 関連するPDBエントリー: 6E8N
• 分子名称: Mammalian ependymin-related protein 1 (1 entity in total)
• 機能のキーワード: lola fold, lysosomal protein, secreted protein, lipid binding, lipid binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 90674.15

構造登録者

Wei, Y.,Prive, G.G. (登録日: 2018-07-27, 公開日: 2019-01-23, 最終更新日: 2024-10-16)

主引用文献

Wei, Y.,Xiong, Z.J.,Li, J.,Zou, C.,Cairo, C.W.,Klassen, J.S.,Prive, G.G.
Crystal structures of human lysosomal EPDR1 reveal homology with the superfamily of bacterial lipoprotein transporters.
Commun Biol, 2:52-52, 2019

PubMed Abstract: EPDR1, a member of the ependymin-related protein family, is a relatively uncharacterized protein found in the lysosomes and secretomes of most vertebrates. Despite having roles in human disease and health, the molecular functions of EPDR1 remain unknown. Here, we present crystal structures of human EPDR1 and reveal that the protein adopts a fold previously seen only in bacterial proteins related to the LolA lipoprotein transporter. EPDR1 forms a homodimer with an overall shape resembling a half-shell with two non-overlapping hydrophobic grooves on the flat side of the hemisphere. EPDR1 can interact with membranes that contain negatively charged lipids, including BMP and GM1, and we suggest that EPDR1 may function as a lysosomal activator protein or a lipid transporter. A phylogenetic analysis reveals that the fold is more widely distributed than previously suspected, with representatives identified in all branches of cellular life.

PubMed: 30729188
DOI: 10.1038/s42003-018-0262-9

実験手法

X-RAY DIFFRACTION (3 Å)