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Journal Article

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

MPS-Authors
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Antonin,  W.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Fasshauer,  D.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Antonin, W., Fasshauer, D., Becker, S., Jahn, R., & Schneider, T. R. (2002). Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs. Nature Structural Biology, 9(2), 107-111. Retrieved from http://www.nature.com/nsmb/journal/v9/n2/pdf/nsb746.pdf.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F459-F
Abstract
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 alpha-helices connected by 16 layers of mostly hydrophobic amino acids. Here we report the 1.9 Angstrom 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.