+Open data
-Basic information
Entry | Database: PDB / ID: 5f0j | ||||||||||||
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Title | Structure of retromer VPS26-VPS35 subunits bound to SNX3 | ||||||||||||
Components |
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Keywords | TRANSPORT PROTEIN / protein transport / retromer / sorting nexin | ||||||||||||
Function / homology | Function and homology information negative regulation of early endosome to late endosome transport / late endosome to Golgi transport / protein to membrane docking / negative regulation of protein transport / positive regulation of locomotion involved in locomotory behavior / neurotransmitter receptor transport, endosome to plasma membrane / regulation of postsynapse assembly / mitochondrion-derived vesicle / negative regulation of protein localization / regulation of dendritic spine maintenance ...negative regulation of early endosome to late endosome transport / late endosome to Golgi transport / protein to membrane docking / negative regulation of protein transport / positive regulation of locomotion involved in locomotory behavior / neurotransmitter receptor transport, endosome to plasma membrane / regulation of postsynapse assembly / mitochondrion-derived vesicle / negative regulation of protein localization / regulation of dendritic spine maintenance / membrane invagination / negative regulation of protein homooligomerization / tubular endosome / mitochondrion to lysosome vesicle-mediated transport / positive regulation of Wnt protein secretion / regulation of terminal button organization / retromer, cargo-selective complex / vesicle-mediated transport in synapse / WNT ligand biogenesis and trafficking / intralumenal vesicle formation / retromer complex binding / negative regulation of late endosome to lysosome transport / negative regulation of lysosomal protein catabolic process / positive regulation of dopamine receptor signaling pathway / positive regulation of dopamine biosynthetic process / retromer complex / mitochondrial fragmentation involved in apoptotic process / phosphatidylinositol-5-phosphate binding / protein localization to endosome / dopaminergic synapse / neurotransmitter receptor transport, endosome to postsynaptic membrane / regulation of synapse maturation / voluntary musculoskeletal movement / negative regulation of viral entry into host cell / regulation of protein metabolic process / phosphatidylinositol-3-phosphate binding / transcytosis / early phagosome / endocytic recycling / regulation of Wnt signaling pathway / retrograde transport, endosome to Golgi / positive regulation of protein localization to cell periphery / regulation of mitochondrion organization / phosphatidylinositol-4-phosphate binding / phosphatidylinositol-3,5-bisphosphate binding / negative regulation of phagocytosis / clathrin-coated vesicle / positive regulation of mitochondrial fission / lysosome organization / regulation of presynapse assembly / D1 dopamine receptor binding / regulation of macroautophagy / response to bacterium / intracellular protein transport / protein destabilization / modulation of chemical synaptic transmission / regulation of protein stability / negative regulation of protein catabolic process / Wnt signaling pathway / positive regulation of neuron projection development / negative regulation of inflammatory response / positive regulation of protein catabolic process / protein transport / positive regulation of canonical Wnt signaling pathway / late endosome / presynapse / early endosome membrane / protein phosphatase binding / vesicle / postsynaptic density / lysosome / early endosome / endosome membrane / Ub-specific processing proteases / endosome / neuron projection / lysosomal membrane / negative regulation of gene expression / neuronal cell body / glutamatergic synapse / positive regulation of gene expression / perinuclear region of cytoplasm / extracellular exosome / cytoplasm / cytosol Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||||||||
Authors | Lucas, M. / Gershlick, D. / Vidaurrazaga, A. / Rojas, A.L. / Bonifacino, J.S. / Hierro, A. | ||||||||||||
Funding support | Spain, 3items
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Citation | Journal: Cell / Year: 2016 Title: Structural Mechanism for Cargo Recognition by the Retromer Complex. Authors: Lucas, M. / Gershlick, D.C. / Vidaurrazaga, A. / Rojas, A.L. / Bonifacino, J.S. / Hierro, A. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5f0j.cif.gz | 209.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5f0j.ent.gz | 162.1 KB | Display | PDB format |
PDBx/mmJSON format | 5f0j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5f0j_validation.pdf.gz | 485.7 KB | Display | wwPDB validaton report |
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Full document | 5f0j_full_validation.pdf.gz | 490.7 KB | Display | |
Data in XML | 5f0j_validation.xml.gz | 33.8 KB | Display | |
Data in CIF | 5f0j_validation.cif.gz | 46.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f0/5f0j ftp://data.pdbj.org/pub/pdb/validation_reports/f0/5f0j | HTTPS FTP |
-Related structure data
Related structure data | 5f0kC 5f0lC 5f0mC 5f0pC 2fauS 2ypsS S: Starting model for refinement C: citing same article (ref.) |
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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
-Vacuolar protein sorting-associated protein ... , 2 types, 2 molecules AB
#1: Protein | Mass: 53288.270 Da / Num. of mol.: 1 / Fragment: Residues 14-470 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: VPS35, MEM3, TCCCTA00141 / Plasmid: pGST-Parallel2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q96QK1 |
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#2: Protein | Mass: 40239.594 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: VPS26A, VPS26 / Plasmid: pmr101A / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O75436 |
-Protein , 1 types, 1 molecules C
#3: Protein | Mass: 19193.814 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SNX3 / Plasmid: pHis-MBP-Parallel2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O60493 |
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-Non-polymers , 4 types, 130 molecules
#4: Chemical | ChemComp-SO4 / #5: Chemical | ChemComp-GOL / #6: Chemical | ChemComp-EDO / #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.56 Å3/Da / Density % sol: 65.46 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6 / Details: 0.9 M AmSO4, 0.1 M MES pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.97893 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 24, 2014 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: Si(111) channel-cut, cryocooled / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97893 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.69→57 Å / Num. obs: 85401 / % possible obs: 98.3 % / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Biso Wilson estimate: 67.063 Å2 / Rmerge F obs: 0.997 / Rmerge(I) obs: 0.09 / Rrim(I) all: 0.107 / Χ2: 1.064 / Net I/σ(I): 12.09 / Num. measured all: 292428 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2FAU, 2YPS Resolution: 2.7→56.98 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.911 / WRfactor Rfree: 0.246 / WRfactor Rwork: 0.2072 / FOM work R set: 0.8343 / SU B: 11.486 / SU ML: 0.224 / SU R Cruickshank DPI: 0.5345 / SU Rfree: 0.3016 / Cross valid method: FREE R-VALUE / σ(F): 0 / ESU R: 0.534 / ESU R Free: 0.302 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 150.07 Å2 / Biso mean: 57.454 Å2 / Biso min: 16.35 Å2
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Refinement step | Cycle: final / Resolution: 2.7→56.98 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.698→2.768 Å / Total num. of bins used: 20
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