Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution

  title={Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 {\AA} resolution},
  author={R B Sutton and Dirk Fasshauer and Reinhard Jahn and Axel T. Brunger},
The evolutionarily conserved SNARE proteins and their complexes are involved in the fusion of vesicles with their target membranes; however, the overall organization and structural details of these complexes are unknown. Here we report the X-ray crystal structure at 2.4 Å resolution of a core synaptic fusion complex containing syntaxin-1A, synaptobrevin-II and SNAP-25B. The structure reveals a highly twisted and parallel four-helix bundle that differs from the bundles described for the… 

Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs.

The main structural features of the neuronal complex are highly conserved during evolution, and it is concluded that fusion-competent SNARE complexes generally consist of four-helix bundles composed of three Q- SNAREs and one R-SNARE.

Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs

The structure of the SNARE core complex is an evolutionarily conserved hallmark of all SNARE complexes and is intimately associated with the general role of SNAREs in membrane fusion.

X-ray Structure of a Neuronal Complexin-SNARE Complex from Squid*

It is proposed that this structure is part of a multiprotein fusion machinery that regulates vesicle fusion at a late pre-fusion stage and may initiate membrane fusion by acting directly or indirectly on complexin, thus allowing the conformational transitions of the trans SNARE complex that are thought to drive membrane fusion.

Self-association of the H3 Region of Syntaxin 1A

Results indicate that Phe-216 has a role in preventing formation of stable parallel helical bundles, thus favoring the interaction of the H3 region of syntaxin 1a with other proteins involved in membrane fusion.

A Novel SNARE N-terminal Domain Revealed by the Crystal Structure of Sec22b*

The 2.4-Å crystal structure of the 130-amino acid N-terminal domain of mouse Sec22b (mSec22b), a SNARE involved in endoplasmic reticulum/Golgi membrane trafficking, is determined and sequence analysis indicates that a similar domain is likely present in the endosomal/lysosomal SNARE VAMP7.

Dynamic Relationship of the SNARE Complex with a Membrane.

Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation

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 that may have important consequences for SNARE complex folding and fusion.

The ionic layer is required for efficient dissociation of the SNARE complex by α-SNAP and NSF

It is proposed that α-SNAP and NSF drive conformational changes at the ionic layer through specific interactions with the syntaxin glutamine, resulting in the dissociation of the SNARE complex.

Structural principles of SNARE complex recognition by the AAA+ protein NSF

The recycling of SNARE proteins following complex formation and membrane fusion is an essential process in eukaryotic trafficking. A highly conserved AAA+ protein, NSF (N-ethylmaleimide sensitive



Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly.

The ternary complex formed from recombinant proteins lacking their membrane anchors revealed a SDS-resistant minimal core, which tends to form an oligomeric species; global analysis of equilibrium ultracentrifugation data suggests a monomer-trimer equilibrium exists.

A Structural Change Occurs upon Binding of Syntaxin to SNAP-25*

Circular dichroism spectroscopy was used here to study the α-helicity of the individual proteins and to gain insight into structural changes associated with complex formation, consistent with induced coiled coil formation upon binding of syntaxin and SNAP-25.

Structural Changes Are Associated with Soluble N-Ethylmaleimide-sensitive Fusion Protein Attachment Protein Receptor Complex Formation*

It is proposed that the transition from largely unstructured monomers to a tightly packed, energetically favored ternary complex connecting two membranes is a key step in overcoming energy barriers for membrane fusion.

Effect of Mutations in Vesicle-Associated Membrane Protein (VAMP) on the Assembly of Multimeric Protein Complexes

A correlation exists between the membrane-trafficking phenotype of the two VAMP-2 point mutants and their competence to form complexes with either syntaxin 1A or SNAP-25.

Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles.

  • H. OttoP. HansonR. Jahn
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1997
Ternary complexes can be assembled and disassembled while all three proteins are anchored as neighbors in the same membrane, suggesting that NSF is involved in priming synaptic vesicles for exocytosis.