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Open data
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Basic information
Entry | Database: PDB / ID: 7nz3 | ||||||
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Title | Cryo-EM structure of apposed MukBEF-MatP monomers on DNA | ||||||
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![]() | DNA BINDING PROTEIN / SMC-kleisin complex / ATPase | ||||||
Function / homology | ![]() nucleoid / chromosome condensation / acyl carrier activity / chromosome segregation / DNA replication / sequence-specific DNA binding / cell division / calcium ion binding / regulation of DNA-templated transcription / DNA binding ...nucleoid / chromosome condensation / acyl carrier activity / chromosome segregation / DNA replication / sequence-specific DNA binding / cell division / calcium ion binding / regulation of DNA-templated transcription / DNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 11 Å | ||||||
![]() | Buermann, F. / Lowe, J. | ||||||
![]() | ![]() Title: Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites. Authors: Frank Bürmann / Louise F H Funke / Jason W Chin / Jan Löwe / ![]() Abstract: The ring-like structural maintenance of chromosomes (SMC) complex MukBEF folds the genome of Escherichia coli and related bacteria into large loops, presumably by active DNA loop extrusion. MukBEF ...The ring-like structural maintenance of chromosomes (SMC) complex MukBEF folds the genome of Escherichia coli and related bacteria into large loops, presumably by active DNA loop extrusion. MukBEF activity within the replication terminus macrodomain is suppressed by the sequence-specific unloader MatP. Here, we present the complete atomic structure of MukBEF in complex with MatP and DNA as determined by electron cryomicroscopy (cryo-EM). The complex binds two distinct DNA double helices corresponding to the arms of a plectonemic loop. MatP-bound DNA threads through the MukBEF ring, while the second DNA is clamped by the kleisin MukF, MukE, and the MukB ATPase heads. Combinatorial cysteine cross-linking confirms this topology of DNA loop entrapment in vivo. Our findings illuminate how a class of near-ubiquitous DNA organizers with important roles in genome maintenance interacts with the bacterial chromosome. #1: ![]() Title: DNA entrapment revealed by the structure of bacterial condensin MukBEF Authors: Buermann, F. / Funke, L.F.H. / Chin, J.W. / Lowe, J. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.9 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 12663MC ![]() 7nywC ![]() 7nyxC ![]() 7nyyC ![]() 7nyzC ![]() 7nz0C ![]() 7nz2C ![]() 7nz4C M: map data used to model this data C: citing same article ( |
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Similar structure data | |
EM raw data | ![]() Data #1: Unaligned multi-frame images of MukBEF(E1407Q)-MatP-DNA in the presence of ATP - Dataset 1 [micrographs - multiframe] Data #2: Unaligned multi-frame images of MukBEF(E1407Q)-MatP-DNA in the presence of ATP - Dataset 2 [micrographs - multiframe] Data #3: Unaligned multi-frame images of MukBEF(E1407Q)-MatP-DNA in the presence of ATP - Dataset 3, grid 1 [micrographs - multiframe] Data #4: Unaligned multi-frame images of MukBEF(E1407Q)-MatP-DNA in the presence of ATP - Dataset 3, grid 2 [micrographs - multiframe] Data #5: Unaligned multi-frame images of MukBEF(E1407Q)-MatP-DNA in the presence of ATP - Dataset 3, grid 3 [micrographs - multiframe]) |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Chromosome partition protein ... , 3 types, 12 molecules A1A2B1B2C1C2D1D2E1E2F1F2
#1: Protein | Mass: 170240.188 Da / Num. of mol.: 4 / Mutation: E1407Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 50193.305 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Protein | Mass: 27423.848 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Protein , 2 types, 8 molecules G1G2H1H2I1I2J1J2
#4: Protein | Mass: 8645.460 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #5: Protein | Mass: 18032.613 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-MatS2 DNA 80 b, oligo ... , 2 types, 4 molecules K1M1L1N1
#6: DNA chain | Mass: 24625.713 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: Synthetic sequence / Source: (synth.) ![]() #7: DNA chain | Mass: 24715.855 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: Synthetic sequence / Source: (synth.) ![]() |
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-Non-polymers , 3 types, 12 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/PNS.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/PNS.gif)
#8: Chemical | ChemComp-MG / #9: Chemical | ChemComp-ATP / #10: Chemical | ChemComp-PNS / |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||||
Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7.3 | ||||||||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
Software | Name: UCSF ChimeraX / Version: 1.1/v9 / Classification: model building / URL: https://www.rbvi.ucsf.edu/chimerax/ / Os: Windows / Type: package |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
3D reconstruction | Resolution: 11 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8561 / Symmetry type: POINT |