6E7O
Crystal structure of deglycosylated human EPDR1
Summary for 6E7O
| Entry DOI | 10.2210/pdb6e7o/pdb |
| Related | 6E8N |
| Descriptor | Mammalian ependymin-related protein 1 (1 entity in total) |
| Functional Keywords | lola fold, lysosomal protein, secreted protein, lipid binding, lipid binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 90674.15 |
| Authors | Wei, Y.,Prive, G.G. (deposition date: 2018-07-27, release date: 2019-01-23, Last modification date: 2024-10-16) |
| Primary citation | 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 Cited by 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: 30729188DOI: 10.1038/s42003-018-0262-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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