MEMBRANE TRANSPORT STRUCTURE FUNCTION AND BIOGENESIS
X-ray Structure of a Neuronal Complexin-SNARE Complex from Squid*

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Nerve terminals release neurotransmitters from vesicles into the synaptic cleft upon transient increases in intracellular Ca2+. This exocytotic process requires the formation of trans SNARE complexes and is regulated by accessory proteins including the complexins. Here we report the crystal structure of a squid core complexin-SNARE complex at 2.95-Å resolution. A helical segment of complexin binds in anti-parallel fashion to the four-helix bundle of the core SNARE complex and interacts at its C terminus with syntaxin and synaptobrevin around the ionic zero layer of the SNARE complex. We propose that this structure is part of a multiprotein fusion machinery that regulates vesicle fusion at a late pre-fusion stage. Accordingly, Ca2+ 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.

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Published, JBC Papers in Press, May 9, 2002, DOI 10.1074/jbc.M203460200

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This work was supported in part by a grant from the European Molecular Biology Laboratory, by Deutsche Forschungsgemeinschaft Grant SFB 474, and by Verband Chemische Industrie.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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Recipient of a European Union Marie Curie fellowship.