2R83
Crystal structure analysis of human synaptotagmin 1 C2A-C2B
Summary for 2R83
| Entry DOI | 10.2210/pdb2r83/pdb |
| Descriptor | Synaptotagmin-1, CHLORIDE ION (3 entities in total) |
| Functional Keywords | c2a-c2b, exocytosis, calcium, cell junction, cytoplasmic vesicle, glycoprotein, lipoprotein, membrane, metal-binding, palmitate, phosphorylation, synapse, transmembrane, endocytosis-exocytosis complex, endocytosis |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass membrane protein : P21579 |
| Total number of polymer chains | 2 |
| Total formula weight | 65352.56 |
| Authors | Sutton, R.B.,Fuson, K.L.,Montes, M.,Robert, J.J. (deposition date: 2007-09-10, release date: 2008-02-12, Last modification date: 2023-08-30) |
| Primary citation | Fuson, K.L.,Montes, M.,Robert, J.J.,Sutton, R.B. Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association. Biochemistry, 46:13041-13048, 2007 Cited by PubMed Abstract: Release of neurotransmitter from synaptic vesicles requires the Ca2+/phospholipid-binding protein synaptotagmin 1. There is considerable evidence that cooperation between the tandem C2 domains of synaptotagmin is a requirement of regulated exocytosis; however, high-resolution structural evidence for this interaction has been lacking. The 2.7 A crystal structure of the cytosolic domains of human synaptotagmin 1 in the absence of Ca2+ reveals a novel closed conformation of the protein. The shared interface between C2A and C2B is stabilized by a network of interactions between residues on the C-terminal alpha-helix of the C2B domain and residues on loops 1-3 of the Ca2+-binding region of C2A. These interactions alter the overall shape of the Ca2+-binding pocket of C2A, but not that of C2B. Thus, synaptotagmin 1 C2A-C2B may utilize a novel regulatory mechanism whereby one C2 domain could regulate the other until an appropriate triggering event decouples them. PubMed: 17956130DOI: 10.1021/bi701651k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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