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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | RUVBL1/2 in complex with ATP | |||||||||
![]() | CryoEM map (Refine3D) for RUVBL1/2-ATP complex | |||||||||
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![]() | RUVBL1 / RUVBL2 / CB-6644 / Inhibitor / Chaperone | |||||||||
Function / homology | ![]() 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 / dynein axonemal particle / Swr1 complex / 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 / dynein axonemal particle / Swr1 complex / RPAP3/R2TP/prefoldin-like complex / regulation of double-strand break repair / positive regulation of telomerase RNA localization to Cajal body / Ino80 complex / protein folding chaperone complex / box C/D snoRNP assembly / regulation of chromosome organization / NuA4 histone acetyltransferase complex / regulation of DNA replication / TFIID-class transcription factor complex binding / regulation of embryonic development / MLL1 complex / Telomere Extension By Telomerase / positive regulation of double-strand break repair via homologous recombination / RNA polymerase II core promoter sequence-specific DNA binding / regulation of DNA repair / Deposition of new CENPA-containing nucleosomes at the centromere / DNA helicase activity / positive regulation of DNA repair / TBP-class protein binding / telomere maintenance / cellular response to estradiol stimulus / Formation of the beta-catenin:TCF transactivating complex / DNA Damage Recognition in GG-NER / euchromatin / negative regulation of canonical Wnt signaling pathway / chromatin DNA binding / ADP binding / beta-catenin binding / nuclear matrix / transcription corepressor activity / UCH proteinases / cellular response to UV / nucleosome / unfolded protein binding / positive regulation of canonical Wnt signaling pathway / protein folding / HATs acetylate histones / ATPase binding / spermatogenesis / regulation of apoptotic process / DNA recombination / DNA helicase / transcription coactivator activity / protein stabilization / Ub-specific processing proteases / regulation of cell cycle / chromatin remodeling / ribonucleoprotein complex / cadherin binding / cell cycle / 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 / protein homodimerization activity / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.26 Å | |||||||||
![]() | Lopez-Perrote A / Llorca O / Garcia-Martin C | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Mechanism of allosteric inhibition of RUVBL1-RUVBL2 by the small-molecule CB-6644 Authors: Garcia-Martin C / Lopez-Perrote A / Boskovic J / Llorca O | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 79.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 22.6 KB 22.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.7 KB | Display | ![]() |
Images | ![]() | 585.7 KB | ||
Filedesc metadata | ![]() | 7.1 KB | ||
Others | ![]() ![]() ![]() | 10 MB 78.9 MB 78.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 932.7 KB | Display | ![]() |
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Full document | ![]() | 932.2 KB | Display | |
Data in XML | ![]() | 17.7 KB | Display | |
Data in CIF | ![]() | 23.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9emcMC ![]() 9emaC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | CryoEM map (Refine3D) for RUVBL1/2-ATP complex | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.8272 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Sharpened map (Postprocess) for RUVBL1/2-ATP complex
File | emd_19817_additional_1.map | ||||||||||||
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Annotation | Sharpened map (Postprocess) for RUVBL1/2-ATP complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 1 (unfiltered) for RUVBL1/2-ATP complex
File | emd_19817_half_map_1.map | ||||||||||||
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Annotation | Half map 1 (unfiltered) for RUVBL1/2-ATP complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 2 (unfiltered) for RUVBL1/2-ATP complex
File | emd_19817_half_map_2.map | ||||||||||||
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Annotation | Half map 2 (unfiltered) for RUVBL1/2-ATP complex | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Hetero-hexameric RUVBL1-RUVBL2 complex bound to ATP and the CB-66...
Entire | Name: Hetero-hexameric RUVBL1-RUVBL2 complex bound to ATP and the CB-6644 inhibitor |
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Components |
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-Supramolecule #1: Hetero-hexameric RUVBL1-RUVBL2 complex bound to ATP and the CB-66...
Supramolecule | Name: Hetero-hexameric RUVBL1-RUVBL2 complex bound to ATP and the CB-6644 inhibitor type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 310.47 kDa/nm |
-Macromolecule #1: RuvB-like 1
Macromolecule | Name: RuvB-like 1 / type: protein_or_peptide / ID: 1 Details: Sequence contains three extra aminoacids (GSH) at the N-terminus due to protease cleavage that do not affect the structure and activity of the protein Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 50.579188 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GSHMKIEEVK STTKTQRIAS HSHVKGLGLD ESGLAKQAAS GLVGQENARE ACGVIVELIK SKKMAGRAVL LAGPPGTGKT ALALAIAQE LGSKVPFCPM VGSEVYSTEI KKTEVLMENF RRAIGLRIKE TKEVYEGEVT ELTPCETENP MGGYGKTISH V IIGLKTAK ...String: GSHMKIEEVK STTKTQRIAS HSHVKGLGLD ESGLAKQAAS GLVGQENARE ACGVIVELIK SKKMAGRAVL LAGPPGTGKT ALALAIAQE LGSKVPFCPM VGSEVYSTEI KKTEVLMENF RRAIGLRIKE TKEVYEGEVT ELTPCETENP MGGYGKTISH V IIGLKTAK GTKQLKLDPS IFESLQKERV EAGDVIYIEA NSGAVKRQGR CDTYATEFDL EAEEYVPLPK GDVHKKKEII QD VTLHDLD VANARPQGGQ DILSMMGQLM KPKKTEITDK LRGEINKVVN KYIDQGIAEL VPGVLFVDEV HMLDIECFTY LHR ALESSI APIVIFASNR GNCVIRGTED ITSPHGIPLD LLDRVMIIRT MLYTPQEMKQ IIKIRAQTEG INISEEALNH LGEI GTKTT LRYSVQLLTP ANLLAKINGK DSIEKEHVEE ISELFYDAKS SAKILADQQD KYMK UniProtKB: RuvB-like 1 |
-Macromolecule #2: RuvB-like 2
Macromolecule | Name: RuvB-like 2 / type: protein_or_peptide / ID: 2 Details: A strectch of 18 extra residues is present at the N-terminus due to cloning design that do not affect the structure and activity of the protein Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 53.047488 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MADLNWISAG HAIADVGTMA TVTATTKVPE IRDVTRIERI GAHSHIRGLG LDDALEPRQA SQGMVGQLAA RRAAGVVLEM IREGKIAGR AVLIAGQPGT GKTAIAMGMA QALGPDTPFT AIAGSEIFSL EMSKTEALTQ AFRRSIGVRI KEETEIIEGE V VEIQIDRP ...String: MADLNWISAG HAIADVGTMA TVTATTKVPE IRDVTRIERI GAHSHIRGLG LDDALEPRQA SQGMVGQLAA RRAAGVVLEM IREGKIAGR AVLIAGQPGT GKTAIAMGMA QALGPDTPFT AIAGSEIFSL EMSKTEALTQ AFRRSIGVRI KEETEIIEGE V VEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QT KFVQCPD GELQKRKEVV HTVSLHEIDV INSRTQGFLA LFSGDTGEIK SEVREQINAK VAEWREEGKA EIIPGVLFID EVH MLDIES FSFLNRALES DMAPVLIMAT NRGITRIRGT SYQSPHGIPI DLLDRLLIVS TTPYSEKDTK QILRIRCEEE DVEM SEDAY TVLTRIGLET SLRYAIQLIT AASLVCRKRK GTEVQVDDIK RVYSLFLDES RSTQYMKEYQ DAFLFNELKG ETMDT S UniProtKB: RuvB-like 2 |
-Macromolecule #3: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 6 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-Macromolecule #4: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 6 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.8 mg/mL | |||||||||||||||
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Buffer | pH: 7.5 Component:
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Grid | Model: Quantifoil R0.6/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 10.0 kPa | |||||||||||||||
Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 90 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Average electron dose: 45.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo |
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Refinement | Space: REAL / Protocol: BACKBONE TRACE |
Output model | ![]() PDB-9emc: |