Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Munc13 structural transitions and oligomers that may choreograph successive stages in vesicle priming for neurotransmitter release.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 119, Issue 7, Year 2022
Publish date	Feb 15, 2022
Authors	Kirill Grushin / R Venkat Kalyana Sundaram / Charles V Sindelar / James E Rothman /
PubMed Abstract	How can exactly six SNARE complexes be assembled under each synaptic vesicle? Here we report cryo-EM crystal structures of the core domain of Munc13, the key chaperone that initiates SNAREpin ...How can exactly six SNARE complexes be assembled under each synaptic vesicle? Here we report cryo-EM crystal structures of the core domain of Munc13, the key chaperone that initiates SNAREpin assembly. The functional core of Munc13, consisting of C1-C2B-MUN-C2C (Munc13C) spontaneously crystallizes between phosphatidylserine-rich bilayers in two distinct conformations, each in a radically different oligomeric state. In the open conformation (state 1), Munc13C forms upright trimers that link the two bilayers, separating them by ∼21 nm. In the closed conformation, six copies of Munc13C interact to form a lateral hexamer elevated ∼14 nm above the bilayer. Open and closed conformations differ only by a rigid body rotation around a flexible hinge, which when performed cooperatively assembles Munc13 into a lateral hexamer (state 2) in which the key SNARE assembly-activating site of Munc13 is autoinhibited by its neighbor. We propose that each Munc13 in the lateral hexamer ultimately assembles a single SNAREpin, explaining how only and exactly six SNARE complexes are templated. We suggest that state 1 and state 2 may represent two successive states in the synaptic vesicle supply chain leading to "primed" ready-release vesicles in which SNAREpins are clamped and ready to release (state 3).
External links	Proc Natl Acad Sci U S A / PubMed:35135883 / PubMed Central
Methods	EM (subtomogram averaging)
Resolution	10.0 Å
Structure data	25737 7t7c EMDB-25737: Subtomogram average of the hexagonal assembly in Munc13-1 C1-C2B-MUN-C2C 2D crystal between lipid bilayers PDB-7t7c: The hexagonal organization of Munc13-1 C1-C2B-MUN-C2C domains between lipid bilayers Method: EM (subtomogram averaging) / Resolution: 10.0 Å 25738 7t7r EMDB-25738: Subtomogram average of Munc13-1 C1-C2B-MUN-C2C trimer within 2D crystal between lipid bilayers. PDB-7t7r: Structure of Munc13-1 C1-C2B-MUN-C2C trimer between lipid bilayers Method: EM (subtomogram averaging) / Resolution: 10.0 Å 25739 7t7v EMDB-25739: Composite map of Lateral Munc13-1 C1-C2B-MUN-C2C molecule PDB-7t7v: Munc13-1 C1-C2B-MUN-C2C Lateral conformation on lipid bilayer surface Method: EM (subtomogram averaging) / Resolution: 10.0 Å 25740 7t7x EMDB-25740: Composite map of Upright Munc13-1 C1-C2B-MUN-C2C molecule spanning two lipid bilayers PDB-7t7x: Munc13-1 C1-C2B-MUN-C2C Upright conformation spanning two lipid bilayers Method: EM (subtomogram averaging) / Resolution: 10.0 Å 25741 7t81 EMDB-25741: A composite 3D map of Munc13-1 C1-C2B-MUN-C2C 2D crystal between lipid bilayers. PDB-7t81: Model of Munc13-1 C1-C2B-MUN-C2C 2D crystal between lipid bilayers. Method: EM (subtomogram averaging) / Resolution: 10.0 Å
Source	rattus norvegicus (Norway rat) mus musculus (house mouse)
Keywords	EXOCYTOSIS / Synaptic Transmission / Munc13 / Membrane Fusion