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Yorodumi- PDB-1urq: Crystal structure of neuronal Q-SNAREs in complex with R-SNARE mo... -
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-Basic information
Entry | Database: PDB / ID: 1urq | ||||||
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Title | Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn | ||||||
Components |
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Keywords | TRANSPORT PROTEIN / TOMOSYN-SNARE COMPLEX / EXOCYTOSIS / FOUR HELICAL BUNDLE / COILED COIL | ||||||
Function / homology | Function and homology information extrinsic component of neuronal dense core vesicle membrane / small GTPase binding => GO:0031267 / BLOC-1 complex / myosin head/neck binding / exocytic insertion of neurotransmitter receptor to postsynaptic membrane / Other interleukin signaling / extrinsic component of presynaptic membrane / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex / synaptobrevin 2-SNAP-25-syntaxin-1a complex / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex ...extrinsic component of neuronal dense core vesicle membrane / small GTPase binding => GO:0031267 / BLOC-1 complex / myosin head/neck binding / exocytic insertion of neurotransmitter receptor to postsynaptic membrane / Other interleukin signaling / extrinsic component of presynaptic membrane / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex / synaptobrevin 2-SNAP-25-syntaxin-1a complex / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex / synaptic vesicle fusion to presynaptic active zone membrane / regulation of synaptic vesicle priming / Glutamate Neurotransmitter Release Cycle / positive regulation of norepinephrine secretion / Norepinephrine Neurotransmitter Release Cycle / Acetylcholine Neurotransmitter Release Cycle / positive regulation of catecholamine secretion / Serotonin Neurotransmitter Release Cycle / GABA synthesis, release, reuptake and degradation / Dopamine Neurotransmitter Release Cycle / regulated exocytosis / presynaptic dense core vesicle exocytosis / ribbon synapse / synaptic vesicle docking / regulation of establishment of protein localization / response to gravity / calcium ion-regulated exocytosis of neurotransmitter / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / vesicle fusion / vesicle docking / acetylcholine-gated channel complex / positive regulation of calcium ion-dependent exocytosis / myosin II binding / chloride channel inhibitor activity / secretion by cell / SNARE complex / SNAP receptor activity / LGI-ADAM interactions / hormone secretion / calcium-ion regulated exocytosis / actomyosin / regulation of exocytosis / positive regulation of hormone secretion / neurotransmitter secretion / neurotransmitter receptor internalization / protein localization to membrane / ATP-dependent protein binding / neurotransmitter transport / insulin secretion / syntaxin-1 binding / SNARE complex assembly / positive regulation of neurotransmitter secretion / syntaxin binding / synaptic vesicle priming / Neutrophil degranulation / regulation of synapse assembly / regulation of neuron projection development / endosomal transport / regulation of synaptic vesicle exocytosis / myosin binding / regulation of protein secretion / exocytosis / voltage-gated potassium channel activity / synaptic vesicle exocytosis / positive regulation of exocytosis / modulation of excitatory postsynaptic potential / associative learning / positive regulation of excitatory postsynaptic potential / protein sumoylation / synaptic vesicle endocytosis / calcium channel inhibitor activity / endomembrane system / long-term memory / axonal growth cone / presynaptic active zone membrane / voltage-gated potassium channel complex / extrinsic component of cytoplasmic side of plasma membrane / somatodendritic compartment / hippocampal mossy fiber to CA3 synapse / photoreceptor inner segment / axonogenesis / GTPase activator activity / SNARE binding / acrosomal vesicle / secretory granule / filopodium / locomotory behavior / long-term synaptic potentiation / postsynaptic density membrane / intracellular protein transport / Schaffer collateral - CA1 synapse / neuron differentiation / trans-Golgi network / positive regulation of insulin secretion / terminal bouton / synaptic vesicle membrane / kinase binding / calcium-dependent protein binding / protein transport / actin cytoskeleton Similarity search - Function | ||||||
Biological species | RATTUS NORVEGICUS (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Pobbati, A. / Razeto, A. / Becker, S. / Fasshauer, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Structural Basis for the Inhibitory Role of Tomosyn in Exocytosis Authors: Pobbati, A. / Razeto, A. / Boddener, M. / Becker, S. / Fasshauer, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1urq.cif.gz | 69.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1urq.ent.gz | 51.5 KB | Display | PDB format |
PDBx/mmJSON format | 1urq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1urq_validation.pdf.gz | 440.7 KB | Display | wwPDB validaton report |
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Full document | 1urq_full_validation.pdf.gz | 442.1 KB | Display | |
Data in XML | 1urq_validation.xml.gz | 14.6 KB | Display | |
Data in CIF | 1urq_validation.cif.gz | 21.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ur/1urq ftp://data.pdbj.org/pub/pdb/validation_reports/ur/1urq | HTTPS FTP |
-Related structure data
Related structure data | 1n7sS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 6686.593 Da / Num. of mol.: 1 / Fragment: RESIDUES 1050-1109 Source method: isolated from a genetically manipulated source Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Cell: NEURON / Organ: BRAIN / Plasmid: PET28A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9Z152, UniProt: Q9WU70*PLUS |
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#2: Protein | Mass: 8711.805 Da / Num. of mol.: 1 / Fragment: T-SNARE COILED-COIL HOMOLOGY, RESIDUES 188-259 Source method: isolated from a genetically manipulated source Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Cell: NEURON / Organ: BRAIN / Plasmid: PET28A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P32851 |
#3: Protein | Mass: 9312.390 Da / Num. of mol.: 1 / Fragment: T-SNARE COILED-COIL HOMOLOGY 1, RESIDUES 7-83 Source method: isolated from a genetically manipulated source Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Cell: NEURON / Organ: BRAIN / Plasmid: PET28A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P13795, UniProt: P60881*PLUS |
#4: Protein | Mass: 7840.723 Da / Num. of mol.: 1 / Fragment: T-SNARE COILED-COIL HOMOLOGY 2, RESIDUES 141-203 Source method: isolated from a genetically manipulated source Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Cell: NEURON / Organ: BRAIN / Plasmid: PGEX-2T / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P13795, UniProt: P60881*PLUS |
#5: Water | ChemComp-HOH / |
Compound details | INVOLVED IN DOCKING OF SYNAPTIC VESICLES AT PRESYNAPTIC ACTIVE ZONES. PLAYS A CRITICAL ROLE IN ...INVOLVED IN DOCKING OF SYNAPTIC VESICLES AT PRESYNAPTI |
Sequence details | THE CONFLICTS THAT ARE SHOWN FOR CHAIN C IN THE DBREF ARISE DUE TO A VARIABE SPLICED ISOFORM OF ...THE CONFLICTS THAT ARE SHOWN FOR CHAIN C IN THE DBREF ARISE DUE TO A VARIABE SPLICED ISOFORM OF P13795. THE VARSPLIC ID FOR THIS IS VSP_006186 AND IS ACCESSIBLE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 48.9 % |
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Crystal grow | pH: 6 / Details: 30% MPD, 50MM CACL2, 50MM MES PH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7A / Wavelength: 0.9184 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Aug 15, 2003 Details: PREMIRROR, DOUBLE CRYSTAL FOCUSSING MONOCHROMATOR, BENT MIRROR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 2→19.39 Å / Num. obs: 21027 / % possible obs: 99.5 % / Redundancy: 3.5 % / Biso Wilson estimate: 24.08429 Å2 / Rmerge(I) obs: 0.051 / Net I/σ(I): 19 |
Reflection shell | Resolution: 2→2.03 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.145 / Mean I/σ(I) obs: 6.4 / % possible all: 97.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1N7S Resolution: 2→19.3892 Å / SU B: 2.209 / SU ML: 0.063 / Cross valid method: THROUGHOUT / ESU R: 0.1529 / ESU R Free: 0.1538
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Displacement parameters | Biso mean: 30.6 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→19.3892 Å
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