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Yorodumi- PDB-1rh8: Three-dimensional structure of the calcium-free Piccolo C2A-domain -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rh8 | ||||||
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Title | Three-dimensional structure of the calcium-free Piccolo C2A-domain | ||||||
Components | Piccolo protein | ||||||
Keywords | METAL BINDING PROTEIN / beta-sandwich | ||||||
Function / homology | Function and homology information rod spherule / regulation of ubiquitin protein ligase activity / presynaptic active zone assembly / presynapse to nucleus signaling pathway / structural constituent of presynaptic active zone / cone cell pedicle / cytoskeleton of presynaptic active zone / ribbon synapse / synaptic vesicle targeting / inhibitory synapse ...rod spherule / regulation of ubiquitin protein ligase activity / presynaptic active zone assembly / presynapse to nucleus signaling pathway / structural constituent of presynaptic active zone / cone cell pedicle / cytoskeleton of presynaptic active zone / ribbon synapse / synaptic vesicle targeting / inhibitory synapse / synaptic vesicle clustering / profilin binding / presynaptic active zone cytoplasmic component / protein localization to synapse / regulation of exocytosis / calcium-dependent phospholipid binding / insulin secretion / parallel fiber to Purkinje cell synapse / Golgi-associated vesicle / presynaptic active zone / GABA-ergic synapse / transport vesicle / cytoskeleton organization / cAMP-mediated signaling / transcription corepressor binding / synapse organization / trans-Golgi network / neuromuscular junction / terminal bouton / growth cone / postsynaptic density / neuron projection / axon / neuronal cell body / glutamatergic synapse / synapse / dendrite / calcium ion binding / perinuclear region of cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Garcia, J. / Gerber, S.H. / Sugita, S. / Sudhof, T.C. / Rizo, J. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2004 Title: A conformational switch in the Piccolo C2A domain regulated by alternative splicing. Authors: Garcia, J. / Gerber, S.H. / Sugita, S. / Sudhof, T.C. / Rizo, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rh8.cif.gz | 897.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rh8.ent.gz | 749.5 KB | Display | PDB format |
PDBx/mmJSON format | 1rh8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rh/1rh8 ftp://data.pdbj.org/pub/pdb/validation_reports/rh/1rh8 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 16479.602 Da / Num. of mol.: 1 / Fragment: C2A-domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: PCLO / Plasmid: PGEX-KG / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9JKS6 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using additional triple resonance experiments. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 150mM NaCl / pH: 6.0 / Pressure: ambient / Temperature: 303 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: The final structures were calculated with a total of 2316 experimental restraints, including 1994 NOE distance restraints, 116 H-bond restraints and 206 torsion angle restraints. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1000 / Conformers submitted total number: 20 |