3HN8
Crystal structure of synaptotagmin
Summary for 3HN8
Entry DOI | 10.2210/pdb3hn8/pdb |
Descriptor | Synaptotagmin-3, CALCIUM ION, ZINC ION (3 entities in total) |
Functional Keywords | synaptotagmin, cell junction, cytoplasmic vesicle, membrane, metal-binding, synapse, transmembrane, signaling protein |
Biological source | Rattus norvegicus (rat) |
Cellular location | Cell membrane ; Single-pass membrane protein : P40748 |
Total number of polymer chains | 3 |
Total formula weight | 100463.19 |
Authors | Strop, P.,Vrljic, M.,Ernst, J.,Brunger, A.T. (deposition date: 2009-05-30, release date: 2010-02-23, Last modification date: 2024-11-20) |
Primary citation | Vrljic, M.,Strop, P.,Ernst, J.A.,Sutton, R.B.,Chu, S.,Brunger, A.T. Molecular mechanism of the synaptotagmin-SNARE interaction in Ca2+-triggered vesicle fusion. Nat.Struct.Mol.Biol., 17:325-331, 2010 Cited by PubMed Abstract: In neurons, SNAREs, synaptotagmin and other factors catalyze Ca(2+)-triggered fusion of vesicles with the plasma membrane. The molecular mechanism of this process, especially the interaction between synaptotagmin and SNAREs, remains an enigma. Here we characterized this interaction by single-molecule fluorescence microscopy and crystallography. The two rigid Ca(2+)-binding domains of synaptotagmin 3 (Syt3) undergo large relative motions in solution. Interaction with SNARE complex amplifies a particular state of the two domains that is further enhanced by Ca(2+). This state is represented by the first SNARE-induced Ca(2+)-bound crystal structure of a synaptotagmin fragment containing both domains. The arrangement of the Ca(2+)-binding loops of this structure of Syt3 matches that of SNARE-bound Syt1, suggesting a conserved feature of synaptotagmins. The loops resemble the membrane-interacting loops of certain viral fusion proteins in the postfusion state, suggesting unexpected similarities between both fusion systems. PubMed: 20173762DOI: 10.1038/nsmb.1764 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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