+Open data
-Basic information
Entry | Database: PDB / ID: 6riq | |||||||||
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Title | MinCD filament from Pseudomonas aeruginosa | |||||||||
Components |
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Keywords | PROTEIN FIBRIL / Bacterial cell division | |||||||||
Function / homology | Function and homology information regulation of cell septum assembly / negative regulation of cell division / division septum assembly / cell morphogenesis / cytoplasmic side of plasma membrane / cell division / ATP hydrolysis activity / ATP binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | Pseudomonas aeruginosa (bacteria) | |||||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Szewczak-Harris, A. / Wagstaff, J. / Lowe, J. | |||||||||
Funding support | United Kingdom, 2items
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Citation | Journal: FEBS Lett / Year: 2019 Title: Cryo-EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution. Authors: Andrzej Szewczak-Harris / James Wagstaff / Jan Löwe / Abstract: Positioning of the division site in many bacterial species relies on the MinCDE system, which prevents the cytokinetic Z-ring from assembling anywhere but the mid-cell, through an oscillatory ...Positioning of the division site in many bacterial species relies on the MinCDE system, which prevents the cytokinetic Z-ring from assembling anywhere but the mid-cell, through an oscillatory diffusion-reaction mechanism. MinD dimers bind to membranes and, via their partner MinC, inhibit the polymerization of cell division protein FtsZ into the Z-ring. MinC and MinD form polymeric assemblies in solution and on cell membranes. Here, we report the high-resolution cryo-EM structure of the copolymeric filaments of Pseudomonas aeruginosa MinCD. The filaments consist of three protofilaments made of alternating MinC and MinD dimers. The MinCD protofilaments are almost completely straight and assemble as single protofilaments on lipid membranes, which we also visualized by cryo-EM. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6riq.cif.gz | 739.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6riq.ent.gz | 627.4 KB | Display | PDB format |
PDBx/mmJSON format | 6riq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6riq_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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Full document | 6riq_full_validation.pdf.gz | 1.9 MB | Display | |
Data in XML | 6riq_validation.xml.gz | 112.5 KB | Display | |
Data in CIF | 6riq_validation.cif.gz | 167.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ri/6riq ftp://data.pdbj.org/pub/pdb/validation_reports/ri/6riq | HTTPS FTP |
-Related structure data
Related structure data | 4897MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 15107.273 Da / Num. of mol.: 11 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: A0A2R4B4N7, UniProt: Q9HYZ7*PLUS #2: Protein | Mass: 29705.143 Da / Num. of mol.: 11 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) Gene: minD, minD_2, ALP65_02808, C0044_24365, C8257_09550, CAZ10_22480, CGU42_07990, DZ940_07140, DZ962_16115, EFK68_22340, EGV95_09885, EGY23_16190, IPC1135_03845, NCTC13719_01733, PAERUG_E15_London_ ...Gene: minD, minD_2, ALP65_02808, C0044_24365, C8257_09550, CAZ10_22480, CGU42_07990, DZ940_07140, DZ962_16115, EFK68_22340, EGV95_09885, EGY23_16190, IPC1135_03845, NCTC13719_01733, PAERUG_E15_London_28_01_14_02879, RW109_RW109_02577 Production host: Escherichia coli (E. coli) / References: UniProt: A0A071KWM5, UniProt: Q9HYZ6*PLUS #3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-ATP / |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: HELICAL ARRAY / 3D reconstruction method: helical reconstruction |
-Sample preparation
Component | Name: MinCD Filament / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Source (natural) | Organism: Pseudomonas aeruginosa (bacteria) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Tecnai Polara / Image courtesy: FEI Company |
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Microscopy | Model: FEI POLARA 300 |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Specimen holder | Cryogen: NITROGEN |
Image recording | Electron dose: 38 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of real images: 3050 |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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Helical symmerty | Angular rotation/subunit: 116.265 ° / Axial rise/subunit: 24.998 Å / Axial symmetry: C1 |
3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 118659 / Symmetry type: HELICAL |
Atomic model building | Protocol: AB INITIO MODEL / Space: RECIPROCAL |