1L4A

X-RAY STRUCTURE OF THE NEURONAL COMPLEXIN/SNARE COMPLEX FROM THE SQUID LOLIGO PEALEI

Summary for 1L4A

• Entry DOI: 10.2210/pdb1l4a/pdb
• Related: 1KIL 1SFC
• Descriptor: SYNAPTOBREVIN, S-SYNTAXIN, S-SNAP25 fusion protein, ... (6 entities in total)
• Functional Keywords: snare, snare complex, membrane fusion, neurotransmission, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Loligo pealei; More
• Cellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein: P47194; Membrane; Lipid-anchor (Potential): Q95PA1
• Total number of polymer chains: 5
• Total formula weight: 47517.12

Authors

Bracher, A.,Kadlec, J.,Betz, H.,Weissenhorn, W. (deposition date: 2002-03-04, release date: 2002-07-31, Last modification date: 2023-08-16)

Primary citation

Bracher, A.,Kadlec, J.,Betz, H.,Weissenhorn, W.
X-ray structure of a neuronal complexin-SNARE complex from squid.
J.Biol.Chem., 277:26517-26523, 2002

PubMed Abstract: Nerve terminals release neurotransmitters from vesicles into the synaptic cleft upon transient increases in intracellular Ca(2+). 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-A 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, Ca(2+) 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.

PubMed: 12004067
DOI: 10.1074/jbc.M203460200

Experimental method

X-RAY DIFFRACTION (2.95 Å)