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Yorodumi- PDB-5dis: Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a... -
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-Basic information
Entry | Database: PDB / ID: 5dis | |||||||||
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Title | Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a 113 amino acid FG-repeat containing fragment of Nup214 | |||||||||
Components |
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Keywords | TRANSPORT PROTEIN / FG-repeats / Nucleoporin / Nup214 / Exportin | |||||||||
Function / homology | Function and homology information cytoplasmic side of nuclear pore / RNA import into nucleus / HuR (ELAVL1) binds and stabilizes mRNA / annulate lamellae / regulation of proteasomal ubiquitin-dependent protein catabolic process / regulation of nucleocytoplasmic transport / RNA cap binding / regulation of centrosome duplication / RNA nuclear export complex / nuclear export signal receptor activity ...cytoplasmic side of nuclear pore / RNA import into nucleus / HuR (ELAVL1) binds and stabilizes mRNA / annulate lamellae / regulation of proteasomal ubiquitin-dependent protein catabolic process / regulation of nucleocytoplasmic transport / RNA cap binding / regulation of centrosome duplication / RNA nuclear export complex / nuclear export signal receptor activity / pre-miRNA export from nucleus / snRNA import into nucleus / Nuclear Pore Complex (NPC) Disassembly / cellular response to mineralocorticoid stimulus / manchette / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / importin-alpha family protein binding / NS1 Mediated Effects on Host Pathways / SUMOylation of SUMOylation proteins / NLS-dependent protein nuclear import complex / regulation of protein export from nucleus / Transport of Mature mRNA Derived from an Intronless Transcript / RNA export from nucleus / structural constituent of nuclear pore / protein localization to nucleolus / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / SUMOylation of RNA binding proteins / Transport of Mature mRNA derived from an Intron-Containing Transcript / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / GTP metabolic process / Postmitotic nuclear pore complex (NPC) reformation / nucleocytoplasmic transport / MicroRNA (miRNA) biogenesis / nuclear import signal receptor activity / Viral Messenger RNA Synthesis / nuclear localization sequence binding / DNA metabolic process / dynein intermediate chain binding / detection of maltose stimulus / maltose binding / maltose transport complex / SUMOylation of ubiquitinylation proteins / maltose transport / maltodextrin transmembrane transport / ribosomal subunit export from nucleus / Vpr-mediated nuclear import of PICs / spermatid development / mitotic sister chromatid segregation / ribosomal small subunit export from nucleus / SUMOylation of DNA replication proteins / carbohydrate transmembrane transporter activity / protein localization to nucleus / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ribosomal large subunit export from nucleus / carbohydrate transport / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / Regulation of HSF1-mediated heat shock response / sperm flagellum / Cajal body / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / mRNA export from nucleus / SUMOylation of DNA damage response and repair proteins / nuclear pore / Cyclin A/B1/B2 associated events during G2/M transition / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / NPAS4 regulates expression of target genes / protein export from nucleus / centriole / viral process / ATP-binding cassette (ABC) transporter complex / SUMOylation of chromatin organization proteins / cell chemotaxis / Downregulation of TGF-beta receptor signaling / mitotic spindle organization / G protein activity / HCMV Late Events / male germ cell nucleus / RHO GTPases Activate Formins / Deactivation of the beta-catenin transactivating complex / hippocampus development / Transcriptional regulation by small RNAs / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / MAPK6/MAPK4 signaling / Heme signaling / ISG15 antiviral mechanism / kinetochore / recycling endosome / small GTPase binding / HCMV Early Events / positive regulation of protein import into nucleus / protein import into nucleus Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å | |||||||||
Authors | Monecke, T. / Port, S.A. / Dickmanns, A. / Kehlenbach, R.H. / Ficner, R. | |||||||||
Funding support | Germany, 1items
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Citation | Journal: Cell Rep / Year: 2015 Title: Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export. Authors: Port, S.A. / Monecke, T. / Dickmanns, A. / Spillner, C. / Hofele, R. / Urlaub, H. / Ficner, R. / Kehlenbach, R.H. #1: Journal: To Be Published Title: Combining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1-RanGTP-SPN1-Nup214 quaternary export complex Authors: Monecke, T. / Dickmanns, A. / Weiss, M.S. / Port, S.A. / Kehlenbach, R.H. / Ficner, R. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5dis.cif.gz | 788.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5dis.ent.gz | 642.6 KB | Display | PDB format |
PDBx/mmJSON format | 5dis.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/di/5dis ftp://data.pdbj.org/pub/pdb/validation_reports/di/5dis | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 4 types, 4 molecules ABCD
#1: Protein | Mass: 120395.742 Da / Num. of mol.: 1 / Fragment: UNP residues 5-1058 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: XPO1, CRM1 / Production host: Escherichia coli (E. coli) / References: UniProt: O14980 |
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#2: Protein | Mass: 19812.088 Da / Num. of mol.: 1 / Fragment: UNP residues 8-179 / Mutation: Q69L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RAN, ARA24, OK/SW-cl.81 / Production host: Escherichia coli (E. coli) / References: UniProt: P62826 |
#3: Protein | Mass: 33276.527 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SNUPN, RNUT1, SPN1 / Production host: Escherichia coli (E. coli) / References: UniProt: O95149 |
#4: Protein | Mass: 50577.461 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (strain K12) (bacteria), (gene. exp.) Homo sapiens (human) Gene: malE, b4034, JW3994, NUP214, CAIN, CAN, KIAA0023 / Production host: Escherichia coli (E. coli) / References: UniProt: P0AEX9, UniProt: P35658 |
-Sugars , 1 types, 1 molecules
#5: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose |
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-Non-polymers , 4 types, 16 molecules
#6: Chemical | #7: Chemical | ChemComp-GTP / | #8: Chemical | ChemComp-MG / | #9: 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: 3.29 Å3/Da / Density % sol: 62.56 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 5% PEG 8000, 0.2M L-proline, 0.1M Tris pH 7.5, 4 mM D-maltose, 180 mM LiCl |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 28, 2014 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: Si111-DCM with sagital bender / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.85→48.49 Å / Num. obs: 67922 / % possible obs: 98.2 % / Observed criterion σ(I): -3 / Redundancy: 4.6 % / Biso Wilson estimate: 80.01 Å2 / Rmerge F obs: 0.999 / Rmerge(I) obs: 0.055 / Rrim(I) all: 0.062 / Χ2: 1.037 / Net I/σ(I): 15.52 / Num. measured all: 313050 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: 0
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3GJX, 1ANF Resolution: 2.85→48.485 Å / SU ML: 0.42 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 32.17 / Stereochemistry target values: ML Details: Overall, the electron density map for MBP and especially its N-terminal lobe is of poor quality. This suggests that significant movement of MBP in the crystal lattice is possible, which is ...Details: Overall, the electron density map for MBP and especially its N-terminal lobe is of poor quality. This suggests that significant movement of MBP in the crystal lattice is possible, which is consistent with the overall elevated B-factors of the MBP residues. Hence, several parts of MBP are not defined in the electron density map. Since dissolved crystals analysed by SDS-PAGE clearly showed the presence of full-length MBP in order to retain structural integrity of the crystal lattice and the MBP, the residues were not omitted.
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Solvent computation | Shrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.85→48.485 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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