Nature Structural Biology9, 107 - 111 (2002)
Published online: 14 January 2002; | doi:10.1038/nsb746
Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs
Wolfram Antonin1, Dirk Fasshauer1, Stefan Becker2, Reinhard Jahn1
& Thomas R. Schneider3
1
Department of Neurobiology and Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
2
NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
3
University of Göttingen, Department of Structural Chemistry, Tammannstrasse 4, 37077 Göttingen, Germany.
Correspondence should be addressed to Reinhard Jahn rjahn@gwdg.de
SNARE proteins are crucial for intracellular membrane fusion in all eukaryotes. These proteins assemble into tight complexes that connect membranes and may induce fusion. The crystal structure of the neuronal core complex is represented by an unusually long bundle of four -helices connected by 16 layers of mostly hydrophobic amino acids. Here we report the 1.9 Å resolution crystal structure of an endosomal SNARE core complex containing four SNAREs: syntaxin 7, syntaxin 8, vti1b and endobrevin/VAMP-8. Despite limited sequence homology, the helix alignment and the layer structure of the endosomal complex are remarkably similar to those of the neuronal complex. However, subtle variations are evident that characterize different SNARE subfamilies. We conclude that 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.
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-helices connected by 16 layers of mostly hydrophobic amino acids. Here we report the 1.9 Å resolution crystal structure of an endosomal SNARE core complex containing four SNAREs: syntaxin 7, syntaxin 8, vti1b and endobrevin/VAMP-8. Despite limited sequence homology, the helix alignment and the layer structure of the endosomal complex are remarkably similar to those of the neuronal complex. However, subtle variations are evident that characterize different SNARE subfamilies. We conclude that 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.
