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| | <StructureSection load='6e8n' size='340' side='right'caption='[[6e8n]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='6e8n' size='340' side='right'caption='[[6e8n]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6e8n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E8N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e8n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E8N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e7o|6e7o]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPDR1, MERP1, UCC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8n OCA], [https://pdbe.org/6e8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e8n RCSB], [https://www.ebi.ac.uk/pdbsum/6e8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8n ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8n OCA], [http://pdbe.org/6e8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e8n RCSB], [http://www.ebi.ac.uk/pdbsum/6e8n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EPDR1_HUMAN EPDR1_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Prive, G G]] | + | [[Category: Prive GG]] |
| - | [[Category: Wei, Y]] | + | [[Category: Wei Y]] |
| - | [[Category: Lipid binding]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Lola fold]]
| + | |
| - | [[Category: Lysosomal protein]]
| + | |
| - | [[Category: Secreted protein]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wei Y, Xiong ZJ, Li J, Zou C, Cairo CW, Klassen JS, Prive GG. Crystal structures of human lysosomal EPDR1 reveal homology with the superfamily of bacterial lipoprotein transporters. Commun Biol. 2019 Feb 5;2:52. doi: 10.1038/s42003-018-0262-9. eCollection 2019. PMID:30729188 doi:http://dx.doi.org/10.1038/s42003-018-0262-9
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