6IYB
Structure of human ORP1 ANK - Rab7 complex
Summary for 6IYB
| Entry DOI | 10.2210/pdb6iyb/pdb |
| Descriptor | Ras-related protein Rab-7a, Oxysterol-binding protein-related protein 1, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | oxysterol-binding protein, orp1, membrane contact site, rab7, ankyrin repeat, cholesterol, rilp, late endosome, transport protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 80190.65 |
| Authors | |
| Primary citation | Tong, J.,Tan, L.,Chun, C.,Im, Y.J. Structural basis of human ORP1-Rab7 interaction for the late-endosome and lysosome targeting. PLoS ONE, 14:e0211724-e0211724, 2019 Cited by PubMed Abstract: Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) constitute a family of lipid transfer proteins conserved in eukaryotes. ORP1 transports cholesterol at the interface between the late endosomes/lysosomes (LELs) and the endoplasmic reticulum (ER). ORP1 is targeted to the endosomal membranes by forming a tripartite complex with the LE GTPase Rab7 and its effector RILP (Rab7-interacting lysosomal protein). Here, we determined the crystal structure of human ORP1 ANK domain in complex with the GTP-bound form of Rab7. ORP1 ANK binds to the helix α3 of Rab7 located away from the switching regions, which makes the interaction independent of the nucleotide-binding state of Rab7. Thus, the effector-interacting switch regions of Rab7 are accessible for RILP binding, allowing formation of the ORP1-Rab7-RILP complex. ORP1 ANK binds to Rab7 and the Rab7-RILP complex with similar micro-molar affinities, which is consistent with the independence binding of ORP1 and RILP to Rab7. The structural model of the ORP1-Rab7-RILP complex correlates with the recruitment of ORP1 at the LEL-ER interface and the role in lipid transport and regulation. PubMed: 30721249DOI: 10.1371/journal.pone.0211724 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.091 Å) |
Structure validation
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