1JTH
Crystal structure and biophysical properties of a complex between the N-terminal region of SNAP25 and the SNARE region of syntaxin 1a
Summary for 1JTH
| Entry DOI | 10.2210/pdb1jth/pdb |
| Related | 1DN1 1HVV 1SFC |
| Descriptor | SNAP25, syntaxin 1a (3 entities in total) |
| Functional Keywords | coiled-coil, polar layer, endocytosis-exocytosis complex, endocytosis/exocytosis |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 4 |
| Total formula weight | 37256.14 |
| Authors | Misura, K.M.S.,Gonzalez Jr., L.C.,May, A.P.,Scheller, R.H.,Weis, W.I. (deposition date: 2001-08-21, release date: 2001-11-28, Last modification date: 2024-03-13) |
| Primary citation | Misura, K.M.,Gonzalez Jr., L.C.,May, A.P.,Scheller, R.H.,Weis, W.I. Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a. J.Biol.Chem., 276:41301-41309, 2001 Cited by PubMed Abstract: SNARE proteins are required for intracellular membrane fusion. In the neuron, the plasma membrane SNAREs syntaxin 1a and SNAP25 bind to VAMP2 found on neurotransmitter-containing vesicles. These three proteins contain "SNARE regions" that mediate their association into stable tetrameric coiled-coil structures. Syntaxin 1a contributes one such region, designated H3, and SNAP25 contributes two SNARE regions to the fusogenic complex with VAMP2. Syntaxin 1a H3 (syn1aH3) and SNAP25 can form a stable assembly, which can then be bound by VAMP2 to form the full SNARE complex. Here we show that syn1aH3 can also form a stable but kinetically trapped complex with the N-terminal SNARE region of SNAP25 (S25N). The crystal structure of this complex reveals an extended parallel four-helix bundle similar to that of the core SNARE and the syn1aH3-SNAP25 complexes. The inherent ability of syn1aH3 and S25N to associate stably in vitro implies that the intracellular fusion machinery must prevent formation of, or remove, any non-productive complexes. Comparison with the syn1aH3-SNAP25 complex suggests that the linkage of the N- and C-terminal SNAP25 SNARE regions is kinetically advantageous in preventing formation of the non-productive syn1aH3-S25N complex. We also demonstrate that the syn1aH3-S25N complex can be disassembled by alpha-SNAP and N-ethylmaleimide-sensitive factor. PubMed: 11533035DOI: 10.1074/jbc.M106853200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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