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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | MukEF in complex with the phage protein gp5.9 (focus) | |||||||||
Map data | Primary map | |||||||||
Sample |
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Keywords | SMC complex / Chromosome segregation / DNA mimic / DNA BINDING PROTEIN | |||||||||
| Function / homology | Function and homology informationcondensin complex / nucleoid / chromosome condensation / chromosome segregation / DNA replication / symbiont-mediated suppression of host innate immune response / cell division / calcium ion binding / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() ![]() Escherichia phage T7 (virus) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | |||||||||
Authors | Burmann F / Wilkinson O / Kimanius D / Dillingham M / Lowe J | |||||||||
| Funding support | European Union, United Kingdom, 2 items
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Citation | Journal: Cell / Year: 2025Title: Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic. Authors: Frank Bürmann / Bryony Clifton / Sophie Koekemoer / Oliver J Wilkinson / Dari Kimanius / Mark S Dillingham / Jan Löwe / ![]() Abstract: Ring-like structural maintenance of chromosome (SMC) complexes are crucial for genome organization and operate through mechanisms of DNA entrapment and loop extrusion. Here, we explore the DNA ...Ring-like structural maintenance of chromosome (SMC) complexes are crucial for genome organization and operate through mechanisms of DNA entrapment and loop extrusion. Here, we explore the DNA loading process of the bacterial SMC complex MukBEF. Using cryoelectron microscopy (cryo-EM), we demonstrate that ATP binding opens one of MukBEF's three potential DNA entry gates, exposing a DNA capture site that positions DNA at the open neck gate. We discover that the gp5.9 protein of bacteriophage T7 blocks this capture site by DNA mimicry, thereby preventing DNA loading and inactivating MukBEF. We propose a comprehensive and unidirectional loading mechanism in which DNA is first captured at the complex's periphery and then ingested through the DNA entry gate, powered by a single cycle of ATP hydrolysis. These findings illuminate a fundamental aspect of how ubiquitous DNA organizers are primed for genome maintenance and demonstrate how this process can be disrupted by viruses. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_51448.map.gz | 32.7 MB | EMDB map data format | |
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| Header (meta data) | emd-51448-v30.xml emd-51448.xml | 23.1 KB 23.1 KB | Display Display | EMDB header |
| Images | emd_51448.png | 41.2 KB | ||
| Masks | emd_51448_msk_1.map | 35.3 MB | Mask map | |
| Filedesc metadata | emd-51448.cif.gz | 6.5 KB | ||
| Others | emd_51448_additional_1.map.gz emd_51448_half_map_1.map.gz emd_51448_half_map_2.map.gz | 32.4 MB 27.3 MB 27.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51448 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51448 | HTTPS FTP |
-Validation report
| Summary document | emd_51448_validation.pdf.gz | 809.9 KB | Display | EMDB validaton report |
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| Full document | emd_51448_full_validation.pdf.gz | 809.4 KB | Display | |
| Data in XML | emd_51448_validation.xml.gz | 10.7 KB | Display | |
| Data in CIF | emd_51448_validation.cif.gz | 12.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51448 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51448 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9gmdMC ![]() 9gm6C ![]() 9gm7C ![]() 9gm8C ![]() 9gm9C ![]() 9gmaC ![]() 9gmbC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_51448.map.gz / Format: CCP4 / Size: 35.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Primary map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.42293 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_51448_msk_1.map | ||||||||||||
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-Additional map: Sharpened map
| File | emd_51448_additional_1.map | ||||||||||||
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| Annotation | Sharpened map | ||||||||||||
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| Density Histograms |
-Half map: Half-map 1
| File | emd_51448_half_map_1.map | ||||||||||||
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| Annotation | Half-map 1 | ||||||||||||
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-Half map: Half-map 2
| File | emd_51448_half_map_2.map | ||||||||||||
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| Annotation | Half-map 2 | ||||||||||||
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Sample components
-Entire : Reconstituted complex of gp5.9/MukEF
| Entire | Name: Reconstituted complex of gp5.9/MukEF |
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| Components |
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-Supramolecule #1: Reconstituted complex of gp5.9/MukEF
| Supramolecule | Name: Reconstituted complex of gp5.9/MukEF / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 233 KDa |
-Macromolecule #1: Chromosome partition protein MukF
| Macromolecule | Name: Chromosome partition protein MukF / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 50.635727 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSEFSQTVPE LVAWARKNDF SISLPVDRLS FLLAVATLNG ERLDGEMSEG ELVDAFRHVS DAFEQTSETI GVRANNAIND MVRQRLLNR FTSEQAEGNA IYRLTPLGIG ITDYYIRQRE FSTLRLSMQL SIVAGELKRA ADAAEEGGDE FHWHRNVYAP L KYSVAEIF ...String: MSEFSQTVPE LVAWARKNDF SISLPVDRLS FLLAVATLNG ERLDGEMSEG ELVDAFRHVS DAFEQTSETI GVRANNAIND MVRQRLLNR FTSEQAEGNA IYRLTPLGIG ITDYYIRQRE FSTLRLSMQL SIVAGELKRA ADAAEEGGDE FHWHRNVYAP L KYSVAEIF DSIDLTQRLM DEQQQQVKDD IAQLLNKDWR AAISSCELLL SETSGTLREL QDTLEAAGDK LQANLLRIQD AT MTHDDLH FVDRLVFDLQ SKLDRIISWG QQSIDLWIGY DRHVHKFIRT AIDMDKNRVF AQRLRQSVQT YFDEPWALTY ANA DRLLDM RDEEMALRDE EVTGELPEDL EYEEFNEIRE QLAAIIEEQL AVYKTRQVPL DLGLVVREYL SQYPRARHFD VARI VIDQA VRLGVAQADF TGLPAKWQPI NDYGAKVQAH VIDKY UniProtKB: Chromosome partition protein MukF |
-Macromolecule #2: Chromosome partition protein MukE
| Macromolecule | Name: Chromosome partition protein MukE / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 27.006484 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSSTNIEQVM PVKLAQALAN PLFPALDSAL RSGRHIGLDE LDNHAFLMDF QEYLEEFYAR YNVELIRAPE GFFYLRPRST TLIPRSVLS ELDMMVGKIL CYLYLSPERL ANEGIFTQQE LYDELLTLAD EAKLLKLVNN RSTGSDVDRQ KLQEKVRSSL N RLRRLGMV ...String: MSSTNIEQVM PVKLAQALAN PLFPALDSAL RSGRHIGLDE LDNHAFLMDF QEYLEEFYAR YNVELIRAPE GFFYLRPRST TLIPRSVLS ELDMMVGKIL CYLYLSPERL ANEGIFTQQE LYDELLTLAD EAKLLKLVNN RSTGSDVDRQ KLQEKVRSSL N RLRRLGMV WFMGHDSSKF RITESVFRFG ADVRAGDDPR EAQRRLIRDG EAMPIENHLQ LNDETEENQP DSGEEE UniProtKB: Chromosome partition protein MukE |
-Macromolecule #3: Probable RecBCD inhibitor gp5.9
| Macromolecule | Name: Probable RecBCD inhibitor gp5.9 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Escherichia phage T7 (virus) |
| Molecular weight | Theoretical: 6.260819 KDa |
| Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
| Sequence | String: GPGMSRDLVT IPRDVWNDIQ GYIDSLEREN DSLKNQLMEA DEYVAELEEK LNGTS UniProtKB: Probable RecBCD inhibitor gp5.9 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7 |
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| Grid | Model: Quantifoil R2/2 / Material: COPPER/RHODIUM / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY |
| Vitrification | Cryogen name: NITROGEN / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Detector mode: COUNTING / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 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
| Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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| Output model | ![]() PDB-9gmd: |
Movie
Controller
About Yorodumi




Keywords

Escherichia phage T7 (virus)
Authors
United Kingdom, 2 items
Citation













Z (Sec.)
Y (Row.)
X (Col.)




















































Trichoplusia ni (cabbage looper)
FIELD EMISSION GUN
