1URQ: Neuronal Q-SNAREs

Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Aug 2004.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: RATTUS NORVEGICUS
Chains: 4
Atoms: 2,249
Mol. weight: 32.55 kDa
Released: 26 Aug 2004

Explore 1URQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1URQ contains 4 α-helices and 0 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1053-1107	55

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	197-256	60

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	17-80	64

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	140-197	58

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
M-tomosyn isoform	A	protein	63	RATTUS NORVEGICUS	Q9WU70 (AlphaFold model)
Syntaxin 1A	B	protein	75	RATTUS NORVEGICUS	P32851 (AlphaFold model)
Synaptosomal-associated protein 25	C	protein	80	RATTUS NORVEGICUS	P60881 (AlphaFold model)
Synaptosomal-associated protein 25	D	protein	69	RATTUS NORVEGICUS	P60881 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1URQ_1 M-TOMOSYN ISOFORM (chains A)
GSHGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMML
KYK

Sequence of entity 2 (B), FASTA

>1URQ_2 SYNTAXIN 1A (chains B)
GSHSKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYV
ERAVSDTKKAVKYQS

Sequence of entity 3 (C), FASTA

>1URQ_3 SYNAPTOSOMAL-ASSOCIATED PROTEIN 25 (chains C)
GSHMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLDRVEEG
MNHINQDMKEAEKNLKDLGK

Sequence of entity 4 (D), FASTA

>1URQ_4 SYNAPTOSOMAL-ASSOCIATED PROTEIN 25 (chains D)
GSHMASRENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEA
NQRATKMLG

Primary citation

Structural Basis for the Inhibitory Role of Tomosyn in Exocytosis. Pobbati, A., Razeto, A., Boddener, M. et al. J Biol Chem (2004) 279:47192. DOI 10.1074/JBC.M408767200 · PubMed

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