1URQ
Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn
Summary for 1URQ
| Entry DOI | 10.2210/pdb1urq/pdb |
| Related | 1BR0 1DN1 1EZ3 1HVV 1JTH 1KIL 1N7S 1SFC 2BU0 |
| Descriptor | M-TOMOSYN ISOFORM, SYNTAXIN 1A, SYNAPTOSOMAL-ASSOCIATED PROTEIN 25, ... (5 entities in total) |
| Functional Keywords | transport protein, tomosyn-snare complex, exocytosis, four helical bundle, coiled coil |
| Biological source | RATTUS NORVEGICUS (RAT) More |
| Total number of polymer chains | 4 |
| Total formula weight | 32551.51 |
| Authors | Pobbati, A.,Razeto, A.,Becker, S.,Fasshauer, D. (deposition date: 2003-10-31, release date: 2004-08-26, Last modification date: 2023-12-13) |
| Primary citation | Pobbati, A.,Razeto, A.,Boddener, M.,Becker, S.,Fasshauer, D. Structural Basis for the Inhibitory Role of Tomosyn in Exocytosis J.Biol.Chem., 279:47192-, 2004 Cited by PubMed Abstract: Upon Ca2+ influx synaptic vesicles fuse with the plasma membrane and release their neurotransmitter cargo into the synaptic cleft. Key players during this process are the Q-SNAREs syntaxin 1a and SNAP-25 and the R-SNARE synaptobrevin 2. It is thought that these membrane proteins gradually assemble into a tight trans-SNARE complex between vesicular and plasma membrane, ultimately leading to membrane fusion. Tomosyn is a soluble protein of 130 kDa that contains a COOH-terminal R-SNARE motif but lacks a transmembrane anchor. Its R-SNARE motif forms a stable core SNARE complex with syntaxin 1a and SNAP-25. Here we present the crystal structure of this core tomosyn SNARE complex at 2.0-A resolution. It consists of a four-helical bundle very similar to that of the SNARE complex containing synaptobrevin. Most differences are found on the surface, where they prevented tight binding of complexin. Both complexes form with similar rates as assessed by CD spectroscopy. In addition, synaptobrevin cannot displace the tomosyn helix from the tight complex and vice versa, indicating that both SNARE complexes represent end products. Moreover, data bank searches revealed that the R-SNARE motif of tomosyn is highly conserved throughout all eukaryotic kingdoms. This suggests that the formation of a tight SNARE complex is important for the function of tomosyn. PubMed: 15316007DOI: 10.1074/JBC.M408767200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
