2KOG
lipid-bound synaptobrevin solution NMR structure
Summary for 2KOG
| Entry DOI | 10.2210/pdb2kog/pdb |
| Descriptor | Vesicle-associated membrane protein 2 (1 entity in total) |
| Functional Keywords | synaptobrevin, vamp2, dpc micelle, snare, coiled coil, membrane fusion, transmembrane, synaptic vesicle, membrane protein |
| Biological source | Rattus norvegicus (rat) |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein: P63045 |
| Total number of polymer chains | 1 |
| Total formula weight | 12986.01 |
| Authors | Ellena, J.F.,Liang, B.,Wiktor, M.,Stein, A.,Cafiso, D.S.,Jahn, R.,Tamm, L.K. (deposition date: 2009-09-22, release date: 2009-12-01, Last modification date: 2024-05-22) |
| Primary citation | Ellena, J.F.,Liang, B.,Wiktor, M.,Stein, A.,Cafiso, D.S.,Jahn, R.,Tamm, L.K. Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. Proc.Natl.Acad.Sci.USA, 106:20306-20311, 2009 Cited by PubMed Abstract: The synaptic vesicle protein synaptobrevin engages with syntaxin and SNAP-25 to form the SNARE complex, which drives membrane fusion in neuronal exocytosis. In the SNARE complex, the SNARE motif of synaptobrevin forms a 55-residue helix, but it has been assumed to be mostly unstructured in its prefusion form. NMR data for full-length synaptobrevin in dodecylphosphocholine micelles reveals two transient helical segments flanked by natively disordered regions and a third more stable helix. Transient helix I comprises the most N-terminal part of the SNARE motif, transient helix II extends the SNARE motif into the juxtamembrane region, and the more stable helix III is the transmembrane domain. These helices may have important consequences for SNARE complex folding and fusion: helix I likely forms a nucleation site, the C-terminal disordered SNARE motif may act as a folding arrest signal, and helix II likely couples SNARE complex folding and fusion. PubMed: 19918058DOI: 10.1073/pnas.0908317106 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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