6e8n

Crystal structure of glycosylated human EPDR1

spinqualitylabelsall models 6e8n, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6e8n is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: 2PE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EPDR1_HUMAN Publication Abstract from PubMed 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. Crystal structures of human lysosomal EPDR1 reveal homology with the superfamily of bacterial lipoprotein transporters.,Wei Y, Xiong ZJ, Li J, Zou C, Cairo CW, Klassen JS, Prive GG Commun Biol. 2019 Feb 5;2:52. doi: 10.1038/s42003-018-0262-9. eCollection 2019. PMID:30729188 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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