Structural Research of SNARE Protein Family

Inquiry

Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) are a family of small conserved eukaryotic proteins that mediate membrane fusion between organelles and plasma membranes. The most well-researched are SNAREs that mediate the release of neurotransmitter-containing synaptic vesicles in neurons. These neuronal traps are targets of neurotoxins produced by certain bacteria that cause botulism and tetanus.

Structural analysis of SNARE

SNAREs play essential roles in vesicular transport and are usually inserted post-translationally into membranes via C-terminal transmembrane structural domains, including insertion into the plasma membrane, endoplasmic reticulum, mitochondria, peroxisomes, etc. SNAREs are targeted by altering the composition of the amino acid residues flanking the C-terminus or the length of the transmembrane structural domains. Although SNAREs vary greatly in structure and size, they all contain a SNARE motif of 60-70 amino acids in their cytoplasmic domains and heptameric repeats capable of forming convoluted helices. v- and t-SNAREs can be reversibly assembled into tightly packed four-helix "trans"-SNARE complexes. SNARE complexes.

Structural resolution of synaptotagmin-1 and neuronal SNARE complexes

Using diffraction data from an X-ray free-electron laser, researchers have determined atomic-resolution structures of synaptotagmin-1 and neuronal SNARE complexes with precise side-chain spindle assignments. The crystal structure of Syt1-SNARE reveals three interfaces between the SNARE complex and the Syt1 C2A and C2B structural domains. In the long-cell form, two instances of essentially identical primary interfaces are formed between the Syt1 C2B structural domain and the SNARE complex. The secondary interface involves another Syt1 C2B structural domain and the SNARE complex, while the tertiary interface involves the Syt1 C2A structural domain and the SNARE complex. The C2A structural domains forming the tertiary interface have the same orientation in both crystal forms and the interacting side chains are located in similar positions.

Figure 1. Crystal structure of the Syt1–SNARE complex. (Zhou Q, et al., 2015)

Protein	Organism	Method	Resolution	PDB Entry ID
SM Protein Vps45 in Complex with Qa SNARE Tlg2 (1-310)	Thermochaetoides thermophila	X-ray diffraction	3.9 Å	6XMD
SM Protein Vps45 in Complex with Qa SNARE Tlg2	Thermochaetoides thermophila	X-ray diffraction	2.8 Å	6XM1
A complex between the SNARE Vam3 and the HOPS Vps33-Vps16 subcomplex	Thermochaetoides thermophila DSM 1495	X-ray diffraction	3.1 Å	5BUZ
A complex between the SNARE Nyv1 and the HOPS Vps33-Vps16 subcomplex	Thermochaetoides thermophila DSM 1495	X-ray diffraction	3.1 Å	5BV0
Vps33-Vps16 Complex	Thermochaetoides thermophila DSM 1495	X-ray diffraction	2.902 Å	5BV1
Syntaxin 6	Rattus norvegicus	X-ray diffraction	2.1 Å	1LVF
SM protein Vps45	Thermochaetoides thermophila	X-ray diffraction	2 Å	6XJL
The vesicular transport protein Sec17	Saccharomyces cerevisiae	X-ray diffraction	2.9 Å	1QQE
NSF-D1D2 part in the whole 20S complex	Cricetulus griseus	Cryo-EM single particle analysis	3.7 Å	6IP2
STX17 LIR region in complex with GABARAP	Homo sapiens	X-ray diffraction	2 Å	7BV4
ATP-bound N-ethylmaleimide sensitive factor	Cricetulus griseus	Cryo-EM single particle analysis	4.2 Å	3J94
The neuronal complexin/snare complex	Doryteuthis pealeii	X-ray diffraction	2.95 Å	1L4A
Autophagic STX17/SNAP29/VAMP8 SNARE complex	Homo sapiens	X-ray diffraction	3.05 Å	7BV6
Unc18-syntaxin 1 complex	Monosiga brevicollis	X-ray diffraction	2.8 Å	2XHE
HOPS component Vps33	Thermochaetoides thermophila DSM 1495	X-ray diffraction	2.6 Å	4JC8
Gamma-SNAP	Danio rerio	X-ray diffraction	2.6 Å	2IFU
Yeast T-SNARE protein SSO1	Saccharomyces cerevisiae	X-ray diffraction	2.1 Å	1FIO
SNARE Sec20 bound to Dsl1 complex subunit Tip20	Eremothecium gossypii ATCC 10895	X-ray diffraction	3.203 Å	6WC3
Sly1 N-terminal domain	Rattus norvegicus	SOLUTION NMR	/	1Y9J
Sro7	Saccharomyces cerevisiae	X-ray diffraction	2.4 Å	2OAJ
Lipid-bound synaptobrevin	Rattus norvegicus	SOLUTION NMR	/	2KOG
Sly1p in complex with an N-terminal peptide of Sed5p	Saccharomyces cerevisiae	X-ray diffraction	3 Å	1MQS
Sec22b N-terminal domain	Mus musculus	X-ray diffraction	2.4 Å	1IFQ
Neuronal SNARE Syntaxin 1A	Rattus norvegicus	SOLUTION NMR	/	2M8R
Neuronal SEC1	Doryteuthis pealeii	X-ray diffraction	2.4 Å	1EPU
ADP-bound N-ethylmaleimide sensitive factor	Cricetulus griseus	Cryo-EM single particle analysis	7.6 Å	3J95
GppNHp-Bound Ypt1p GTPase	Saccharomyces cerevisiae	X-ray diffraction	2.06 Å	1YZN
Mint1/Munc18-1/syntaxin-1 complex	Rattus norvegicus	X-ray diffraction	3.2 Å	7XSJ

Table 1. Structural research of the SNARE protein family.

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References

Zhou Q, et al. Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis. Nature. 2015. 525(7567): 62-67.
Wang T, et al. SNARE proteins in membrane trafficking. Traffic. 2017.18(12): 767-775.
Han J, et al. The Multifaceted Role of SNARE Proteins in Membrane Fusion. Front Physiol. 2017. 8: 5.
Fasshauer D. Structural insights into the SNARE mechanism. Biochim Biophys Acta. 2003.1641(2-3): 87-97.

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