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- EMDB-45043: Filamentous Epstein-Barr virus annealase BALF2 ssDNA-annealing complex -
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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Filamentous Epstein-Barr virus annealase BALF2 ssDNA-annealing complex | |||||||||
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![]() | Recombinase / annealase / SSB / Filament / Homologous Recombination / RECOMBINATION / RECOMBINATION-DNA complex | |||||||||
Function / homology | ![]() viral tegument / bidirectional double-stranded viral DNA replication / single-stranded DNA binding / DNA replication / host cell nucleus Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.75 Å | |||||||||
![]() | Nicholls J / Tolun G / Brewster J | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural determination of BALF2 annealing intermediate reveals the mechanism through which DNA annealing occurs Authors: Nicholls J / Brewster J / Tolun G | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 855.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 24.1 KB 24.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 25.6 KB | Display | ![]() |
Images | ![]() | 25.2 KB | ||
Masks | ![]() | 1.7 GB | ![]() | |
Filedesc metadata | ![]() | 8 KB | ||
Others | ![]() ![]() | 1.6 GB 1.6 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 835.4 KB | Display | ![]() |
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Full document | ![]() | 835 KB | Display | |
Data in XML | ![]() | 33.7 KB | Display | |
Data in CIF | ![]() | 46 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9byrMC ![]() 9bypC ![]() 9byqC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.64063 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_45043_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_45043_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Epstein-Barr virus recombinase BALF2 filamentous ssDNA-annealing ...
Entire | Name: Epstein-Barr virus recombinase BALF2 filamentous ssDNA-annealing complex |
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Components |
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-Supramolecule #1: Epstein-Barr virus recombinase BALF2 filamentous ssDNA-annealing ...
Supramolecule | Name: Epstein-Barr virus recombinase BALF2 filamentous ssDNA-annealing complex type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Major DNA-binding protein
Macromolecule | Name: Major DNA-binding protein / type: protein_or_peptide / ID: 1 / Number of copies: 24 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 123.247445 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MQGAQTSEDN LGSQSQPGPC GYIYFYPLAT YPLREVATLG TGYAGHRCLT VPLLCGITVE PGFSINVKAL HRRPDPNCGL LRATSYHRD IYVFHNAHMV PPIFEGPGLE ALCGETREVF GYDAYSALPR ESSKPGDFFP EGLDPSAYLG AVAITEAFKE R LYSGNLVA ...String: MQGAQTSEDN LGSQSQPGPC GYIYFYPLAT YPLREVATLG TGYAGHRCLT VPLLCGITVE PGFSINVKAL HRRPDPNCGL LRATSYHRD IYVFHNAHMV PPIFEGPGLE ALCGETREVF GYDAYSALPR ESSKPGDFFP EGLDPSAYLG AVAITEAFKE R LYSGNLVA IPSLKQEVAV GQSASVRVPL YDKEVFPEGV PQLRQFYNSD LSRCMHEALY TGLAQALRVR RVGKLVELLE KQ SLQDQAK VAKVAPLKEF PASTISHPDS GALMIVDSAA CELAVSYAPA MLEASHETPA SLNYDSWPLF ADCEGPEARV AAL HRYNAS LAPHVSTQIF ATNSVLYVSG VSKSTGQGKE SLFNSFYMTH GLGTLQEGTW DPCRRPCFSG WGGPDVTGTN GPGN YAVEH LVYAASFSPN LLARYAYYLQ FCQGQKSSLT PVPETGSYVA GAAASPMCSL CEGRAPAVCL NTLFFRLRDR FPPVM STQR RDPYVISGAS GSYNETDFLG NFLNFIDKED DGQRPDDEPR YTYWQLNQNL LERLSRLGID AEGKLEKEPH GPRDFV KMF KDVDAAVDAE VVQFMNSMAK NNITYKDLVK SCYHVMQYSC NPFAQPACPI FTQLFYRSLL TILQDISLPI CMCYEND NP GLGQSPPEWL KGHYQTLCTN FRSLAIDKGV LTAKEAKVVH GEPTCDLPDL DAALQGRVYG RRLPVRMSKV LMLCPRNI K IKNRVVFTGE NAALQNSFIK STTRRENYII NGPYMKFLNT YHKTLFPDTK LSSLYLWHNF SRRRSVPVPS GASAEEYSD LALFVDGGSR AHEESNVIDV VPGNLVTYAK QRLNNAILKA CGQTQFYISL IQGLVPRTQS VPARDYPHVL GTRAVESAAA YAEATSSLT ATTVVCAATD CLSQVCKARP VVTLPVTINK YTGVNGNNQI FQAGNLGYFM GRGVDRNLLQ APGAGLRKQA G GSSMRKKF VFATPTLGLT VKRRTQAATT YEIENIRAGL EAIISQKQEE DCVFDVVCNL VDAMGEACAS LTRDDAEYLL GR FSVLADS VLETLATIAS SGIEWTAEAA RDFLEGVWGG PGAAQDNFIS VAEPVSTASQ ASAGLLLGGG GQGSGGRRKR RLA TVLPGL EV UniProtKB: Major DNA-binding protein |
-Macromolecule #2: DNA(5'-D(*GP*CP*AP*GP*AP*AP*TP*CP*GP*CP*CP*C)-3')
Macromolecule | Name: DNA(5'-D(*GP*CP*AP*GP*AP*AP*TP*CP*GP*CP*CP*C)-3') / type: dna / ID: 2 / Number of copies: 11 / Classification: DNA |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 3.632382 KDa |
Sequence | String: (DG)(DC)(DA)(DG)(DA)(DA)(DT)(DC)(DG)(DC) (DC)(DC) |
-Macromolecule #3: DNA(5'-D(*AP*GP*CP*TP*CP*GP*AP*TP*TP*TP*TP*T)-3')
Macromolecule | Name: DNA(5'-D(*AP*GP*CP*TP*CP*GP*AP*TP*TP*TP*TP*T)-3') / type: dna / ID: 3 / Number of copies: 11 / Classification: DNA |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 3.643388 KDa |
Sequence | String: (DA)(DG)(DC)(DT)(DC)(DG)(DA)(DT)(DT)(DT) (DT)(DT) |
-Macromolecule #4: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 4 / Number of copies: 22 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | filament |
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Sample preparation
Concentration | 0.9 mg/mL | |||||||||||||||
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Buffer | pH: 9 Component:
Details: Sample incubated for 30 minutes at 37 degrees Celsius and then for 20 hours at 4 degrees Celsius, in the presence of 1.83 uM oligonucleotide | |||||||||||||||
Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 120 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.039 kPa Details: Quantifoil R1.2/1.3 + 2nm continuous carbon were also used for collection | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV | |||||||||||||||
Details | The sample formed flexible helical assemblies |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 15 eV |
Details | Preliminary Grid screening was performed manually |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 2 / Number real images: 11747 / Average electron dose: 65.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm |
Sample stage | 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: experimental model Details: Assymetric Unit was determined to a high-resolution via local refinement and then rigid-fit into low-resolution map |
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Details | Protein was rigid-fit using chimeraX |
Refinement | Space: REAL / Protocol: RIGID BODY FIT |
Output model | ![]() PDB-9byr: |