1K5W
THREE-DIMENSIONAL STRUCTURE OF THE SYNAPTOTAGMIN 1 C2B-DOMAIN: SYNAPTOTAGMIN 1 AS A PHOSPHOLIPID BINDING MACHINE
Summary for 1K5W
| Entry DOI | 10.2210/pdb1k5w/pdb |
| NMR Information | BMRB: 5194 |
| Descriptor | Synaptotagmin I, CALCIUM ION (2 entities in total) |
| Functional Keywords | c2b-domain, c2-domain, synaptotagmin i, calcium-binding, phospholipid-binding, synapsis, neurotransmitter release, synaptic vesicle exocytosis, endocytosis-exocytosis complex, endocytosis/exocytosis |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein: P21707 |
| Total number of polymer chains | 1 |
| Total formula weight | 17432.36 |
| Authors | Fernandez, I.,Arac, D.,Ubach, J.,Gerber, S.H.,Shin, O.,Gao, Y.,Anderson, R.G.W.,Sudhof, T.C.,Rizo, J. (deposition date: 2001-10-12, release date: 2002-01-23, Last modification date: 2024-05-22) |
| Primary citation | Fernandez, I.,Arac, D.,Ubach, J.,Gerber, S.H.,Shin, O.,Gao, Y.,Anderson, R.G.,Sudhof, T.C.,Rizo, J. Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine. Neuron, 32:1057-1069, 2001 Cited by PubMed Abstract: Synaptotagmin 1 probably functions as a Ca2+ sensor in neurotransmitter release via its two C2-domains, but no common Ca2+-dependent activity that could underlie a cooperative action between them has been described. The NMR structure of the C2B-domain now reveals a beta sandwich that exhibits striking similarities and differences with the C2A-domain. Whereas the bottom face of the C2B-domain has two additional alpha helices that may be involved in specialized Ca2+-independent functions, the top face binds two Ca2+ ions and is remarkably similar to the C2A-domain. Consistent with these results, but in contrast to previous studies, we find that the C2B-domain binds phospholipids in a Ca2+-dependent manner similarly to the C2A-domain. These results suggest a novel view of synaptotagmin function whereby the two C2-domains cooperate in a common activity, Ca2+-dependent phospholipid binding, to trigger neurotransmitter release. PubMed: 11754837DOI: 10.1016/S0896-6273(01)00548-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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