3RL0

Truncated SNARE complex with complexin (P1)

Summary for 3RL0

• Entry DOI: 10.2210/pdb3rl0/pdb
• Related: 3RK2 3RK3
• Descriptor: Vesicle-associated membrane protein 2, Syntaxin-1A, Synaptosomal-associated protein 25, ... (5 entities in total)
• Functional Keywords: snare proteins, membrane fusion, membrane protein-exocytosis complex, membrane protein/exocytosis
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein: P63027; Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851; Cytoplasm, perinuclear region (By similarity): P60880 P60880; Cytoplasm, cytosol (By similarity): O14810
• Total number of polymer chains: 40
• Total formula weight: 288377.24

Authors

Kuemmel, D.,Reinisch, K.M. (deposition date: 2011-04-19, release date: 2011-07-27, Last modification date: 2011-08-24)

Primary citation

Kummel, D.,Krishnakumar, S.S.,Radoff, D.T.,Li, F.,Giraudo, C.G.,Pincet, F.,Rothman, J.E.,Reinisch, K.M.
Complexin cross-links prefusion SNAREs into a zigzag array.
Nat.Struct.Mol.Biol., 18:927-933, 2011

PubMed Abstract: Complexin prevents SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. To understand the mechanism for this inhibition, we determined the structure of complexin bound to a mimetic of a prefusion SNAREpin lacking the portion of the v-SNARE that zippers last to trigger fusion. The 'central helix' of complexin is anchored to one SNARE complex, while its 'accessory helix' extends away at ~45° and bridges to a second complex, occupying the vacant v-SNARE binding site to inhibit fusion. We expected the accessory helix to compete with the v-SNARE for t-SNARE binding but found instead that the interaction occurs intermolecularly. Thus, complexin organizes the SNAREs into a zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion.

PubMed: 21785414
DOI: 10.1038/nsmb.2101

Experimental method

X-RAY DIFFRACTION (3.8 Å)