6Q9M
Central Fibronectin-III array of RIM-binding protein
Summary for 6Q9M
| Entry DOI | 10.2210/pdb6q9m/pdb |
| Descriptor | RIM-binding protein, isoform F, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | active zone, rim-binding protein, fibronectin type iii, fn-iii, exocytosis |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 2 |
| Total formula weight | 65112.23 |
| Authors | Driller, J.D.,Habibi, S.,Wahl, M.C.,Loll, B. (deposition date: 2018-12-18, release date: 2020-01-15, Last modification date: 2024-05-15) |
| Primary citation | Petzoldt, A.G.,Gotz, T.W.B.,Driller, J.H.,Lutzkendorf, J.,Reddy-Alla, S.,Matkovic-Rachid, T.,Liu, S.,Knoche, E.,Mertel, S.,Ugorets, V.,Lehmann, M.,Ramesh, N.,Beuschel, C.B.,Kuropka, B.,Freund, C.,Stelzl, U.,Loll, B.,Liu, F.,Wahl, M.C.,Sigrist, S.J. RIM-binding protein couples synaptic vesicle recruitment to release sites. J.Cell Biol., 219:-, 2020 Cited by PubMed Abstract: At presynaptic active zones, arrays of large conserved scaffold proteins mediate fast and temporally precise release of synaptic vesicles (SVs). SV release sites could be identified by clusters of Munc13, which allow SVs to dock in defined nanoscale relation to Ca2+ channels. We here show in Drosophila that RIM-binding protein (RIM-BP) connects release sites physically and functionally to the ELKS family Bruchpilot (BRP)-based scaffold engaged in SV recruitment. The RIM-BP N-terminal domain, while dispensable for SV release site organization, was crucial for proper nanoscale patterning of the BRP scaffold and needed for SV recruitment of SVs under strong stimulation. Structural analysis further showed that the RIM-BP fibronectin domains form a "hinge" in the protein center, while the C-terminal SH3 domain tandem binds RIM, Munc13, and Ca2+ channels release machinery collectively. RIM-BPs' conserved domain architecture seemingly provides a relay to guide SVs from membrane far scaffolds into membrane close release sites. PubMed: 32369542DOI: 10.1083/jcb.201902059 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.453 Å) |
Structure validation
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