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Yorodumi- PDB-2xsz: The dodecameric human RuvBL1:RuvBL2 complex with truncated domains II -
+Open data
-Basic information
Entry | Database: PDB / ID: 2xsz | ||||||
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Title | The dodecameric human RuvBL1:RuvBL2 complex with truncated domains II | ||||||
Components |
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Keywords | HYDROLASE / AAA+ PROTEINS / HELICASE / CHROMATIN REMODELLING | ||||||
Function / homology | Function and homology information promoter-enhancer loop anchoring activity / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / establishment of protein localization to chromatin / R2TP complex / Swr1 complex / dynein axonemal particle / RPAP3/R2TP/prefoldin-like complex / regulation of double-strand break repair / positive regulation of telomerase RNA localization to Cajal body ...promoter-enhancer loop anchoring activity / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / establishment of protein localization to chromatin / R2TP complex / Swr1 complex / dynein axonemal particle / RPAP3/R2TP/prefoldin-like complex / regulation of double-strand break repair / positive regulation of telomerase RNA localization to Cajal body / Ino80 complex / box C/D snoRNP assembly / protein folding chaperone complex / NuA4 histone acetyltransferase complex / regulation of chromosome organization / positive regulation of double-strand break repair via homologous recombination / regulation of DNA replication / MLL1 complex / TFIID-class transcription factor complex binding / regulation of embryonic development / Telomere Extension By Telomerase / RNA polymerase II core promoter sequence-specific DNA binding / regulation of DNA repair / Deposition of new CENPA-containing nucleosomes at the centromere / positive regulation of DNA repair / DNA helicase activity / TBP-class protein binding / telomere maintenance / cellular response to estradiol stimulus / ADP binding / Formation of the beta-catenin:TCF transactivating complex / DNA Damage Recognition in GG-NER / negative regulation of canonical Wnt signaling pathway / euchromatin / chromatin DNA binding / beta-catenin binding / nuclear matrix / positive regulation of canonical Wnt signaling pathway / transcription corepressor activity / UCH proteinases / cellular response to UV / nucleosome / unfolded protein binding / protein folding / HATs acetylate histones / ATPase binding / spermatogenesis / regulation of apoptotic process / DNA helicase / DNA recombination / transcription coactivator activity / protein stabilization / regulation of cell cycle / Ub-specific processing proteases / chromatin remodeling / cadherin binding / cell cycle / ribonucleoprotein complex / RNA polymerase II cis-regulatory region sequence-specific DNA binding / cell division / DNA repair / centrosome / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / ATP hydrolysis activity / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / extracellular exosome / nucleoplasm / ATP binding / membrane / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3 Å | ||||||
Authors | Gorynia, S. / Bandeiras, T.M. / Matias, P.M. / Pinho, F.G. / McVey, C.E. / Vonrhein, C. / Svergun, D.I. / Round, A. / Donner, P. / Carrondo, M.A. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2011 Title: Structural and Functional Insights Into a Dodecameric Molecular Machine - the Ruvbl1/Ruvbl2 Complex. Authors: Gorynia, S. / Bandeiras, T.M. / Pinho, F.G. / Mcvey, C.E. / Vonrhein, C. / Round, A. / Svergun, D.I. / Donner, P. / Matias, P.M. / Carrondo, M.A. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2008 Title: Cloning, Expression, Purification, Crystallization and Preliminary X-Ray Analysis of the Human Ruvbl1- Ruvbl2 Complex. Authors: Gorynia, S. / Matias, P.M. / Bandeiras, T.M. / Donner, P. / Carrondo, M.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2xsz.cif.gz | 759.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2xsz.ent.gz | 634.1 KB | Display | PDB format |
PDBx/mmJSON format | 2xsz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xs/2xsz ftp://data.pdbj.org/pub/pdb/validation_reports/xs/2xsz | HTTPS FTP |
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-Related structure data
Related structure data | 2c9oS 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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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 40944.566 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: DOMAIN II WAS TRUNCATED BETWEEN RESIDUES T127 AND E233. A 4-RESIDUE LINKER WITH SEQUENCE GPPG WAS INSERTED TO REPLACE THE DELETED REGION Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PETDUET / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / References: UniProt: Q9Y265, DNA helicase #2: Protein | Mass: 42474.375 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: DOMAIN II WAS TRUNCATED BETWEEN RESIDUES E134 AND E237. A 4-RESIDUE LINKER WITH SEQUENCE GPPG WAS INSERTED TO REPLACE THE DELETED REGION Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PETDUET / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / References: UniProt: Q9Y230, DNA helicase #3: Chemical | ChemComp-ATP / Sequence details | CHAINS A-C TRUNCATED BETWEEN RESIDUES T127 AND E233 CHAINS D-F TRUNCATED BETWEEN RESIDUES E134 AND ...CHAINS A-C TRUNCATED BETWEEN RESIDUES T127 AND E233 CHAINS D-F TRUNCATED BETWEEN RESIDUES E134 AND E237 IN EACH CASE A 4-RESIDUE LINKER WITH SEQUENCE GPPG WAS INSERTED. | |
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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: 2.6 Å3/Da / Density % sol: 53 % Description: THE SE ATOM SUBSTRUCTURE WAS DETERMINED BY MOLECULAR REPLACEMENT. |
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Crystal grow | pH: 7.5 Details: CRYSTALLIZATION DROPS WERE MIXED FROM EQUAL VOLUMES OF PROTEIN SOLUTION (12 MG/ML, 20MM TRIS-HCL PH 8.0, 200MM NACL, 10% GLYCEROL, 4MM MGCL2, 4MM ADP, 0.5MM TCEP) AND CRYSTALLIZATION ...Details: CRYSTALLIZATION DROPS WERE MIXED FROM EQUAL VOLUMES OF PROTEIN SOLUTION (12 MG/ML, 20MM TRIS-HCL PH 8.0, 200MM NACL, 10% GLYCEROL, 4MM MGCL2, 4MM ADP, 0.5MM TCEP) AND CRYSTALLIZATION SOLUTION (0.2M MGCL2, 30% PEG 400, 0.1M HEPES PH 7.5). |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97633 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Feb 12, 2010 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97633 Å / Relative weight: 1 |
Reflection | Resolution: 3→49 Å / Num. obs: 51774 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 99.32 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 12 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.76 / Mean I/σ(I) obs: 1.7 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MAD Starting model: PDB ENTRY 2C9O Resolution: 3→46.14 Å / Cor.coef. Fo:Fc: 0.9462 / Cor.coef. Fo:Fc free: 0.9413 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.316
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Displacement parameters | Biso mean: 111.89 Å2
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Refine analyze | Luzzati coordinate error obs: 0.577 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→46.14 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.08 Å / Total num. of bins used: 20
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Refinement TLS params. | Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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