5z2n | pdb_00005z2n

Structure of Orp1L N-terminal Domain

spinqualitylabelsall models 5z2n, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5z2n is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.14Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OSBL1_MOUSE Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate. Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A. Binds 25-hydroxycholesterol and cholesterol.[UniProtKB:Q9BXW6] Publication Abstract from PubMed Endosomal transport represents the primary mode for intracellular trafficking and signaling transduction and thus has to be tightly controlled. The molecular processes controlling the endosomal positioning utilize several large protein complexes, one of which contains the small GTPase Rab7, Rab-interacting lysosomal protein (RILP), and oxysterol-binding protein-related protein 1 (ORP1L). Rab7 is known to interact with RILP through a canonical binding site termed the effector-interacting switch region, but it is not clear how Rab7 interacts with ORP1L, limiting our understanding of the overall process. Here, we report structural and biochemical investigation of the Rab7-ORP1L interaction. We found that, contrary to prior studies, the interaction between Rab7 and the N-terminal ankyrin repeat domain (ARDN) of ORP1L is independent of Rab7's GTP- or GDP-binding state. Moreover, we show that Rab7 interacts with ORP1L ARDN via a unique region consisting of helix3 (alpha3) and 310-helix 2 (eta2). This architecture leaves the canonical effector-interacting switch regions available for RILP binding and thus allows formation of the ORP1L-Rab7-RILP tripartite complex. Mutational disruption of the interacting interface between ORP1L and Rab7 compromised the ability of ORP1L-Rab7-RILP to regulate the late endosome positioning. Collectively, our results again manifested the versatility in the interaction between GTPase and its effector. A non-canonical GTPase interaction enables ORP1L-Rab7-RILP complex formation and late endosome positioning.,Ma X, Liu K, Li J, Li H, Li J, Liu Y, Yang C, Liang H J Biol Chem. 2018 Sep 7;293(36):14155-14164. doi: 10.1074/jbc.RA118.001854. Epub , 2018 Jul 16. PMID:30012887 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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