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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-0312 | |||||||||
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Title | Structure of McrBC without DNA binding domains (Class 2) | |||||||||
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![]() | AAA+ superfamily / restriction enzyme / DNA BINDING PROTEIN | |||||||||
Function / homology | ![]() type IV site-specific deoxyribonuclease activity / restriction endodeoxyribonuclease activity / endonuclease complex / double-stranded methylated DNA binding / hemi-methylated DNA-binding / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters / DNA catabolic process / DNA restriction-modification system / endonuclease activity / GTPase activity ...type IV site-specific deoxyribonuclease activity / restriction endodeoxyribonuclease activity / endonuclease complex / double-stranded methylated DNA binding / hemi-methylated DNA-binding / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters / DNA catabolic process / DNA restriction-modification system / endonuclease activity / GTPase activity / GTP binding / ATP hydrolysis activity / DNA binding / ATP binding / identical protein binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.3 Å | |||||||||
![]() | Itoh Y / Nirwan N | |||||||||
![]() | ![]() Title: Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC. Authors: Nirwan N / Itoh Y / Singh P / Bandyopadhyay S / Vinothkumar KR / Amunts A / Saikrishnan K | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 7.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.4 KB 20.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.6 KB | Display | ![]() |
Images | ![]() | 302.9 KB | ||
Masks | ![]() | 52.7 MB | ![]() | |
Filedesc metadata | ![]() | 6.7 KB | ||
Others | ![]() ![]() | 39.7 MB 39.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 429 KB | Display | ![]() |
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Full document | ![]() | 428.2 KB | Display | |
Data in XML | ![]() | 14.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6hz6MC ![]() 0310C ![]() 0311C ![]() 0313C ![]() 0314C ![]() 0315C ![]() 6hz4C ![]() 6hz5C ![]() 6hz7C ![]() 6hz8C ![]() 6hz9C M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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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: 1.05 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_0312_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_0312_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : McrB and McrC complex without DNA binding domains
Entire | Name: McrB and McrC complex without DNA binding domains |
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Components |
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-Supramolecule #1: McrB and McrC complex without DNA binding domains
Supramolecule | Name: McrB and McrC complex without DNA binding domains / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 Details: The N-terminal DNA binding domain of McrB is truncated |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 510 KDa |
-Macromolecule #1: 5-methylcytosine-specific restriction enzyme B
Macromolecule | Name: 5-methylcytosine-specific restriction enzyme B / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO EC number: Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 35.758492 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSKTESYCLE DALNDLFIPE TTIETILKRL TIKKNIILQG PPGVGKTFVA RRLAYLLTGE KAPQRVNMVQ FHQSYSYEDF IQGYRPNGV GFRRKDGIFY NFCQQAKEQP EKKYIFIIDE INRANLSKVF GEVMMLMEHD KRGENWSVPL TYSENDEERF Y VPENVYII ...String: MSKTESYCLE DALNDLFIPE TTIETILKRL TIKKNIILQG PPGVGKTFVA RRLAYLLTGE KAPQRVNMVQ FHQSYSYEDF IQGYRPNGV GFRRKDGIFY NFCQQAKEQP EKKYIFIIDE INRANLSKVF GEVMMLMEHD KRGENWSVPL TYSENDEERF Y VPENVYII GLMNTADRSL AVVDYALRRR FSFIDIEPGF DTPQFRNFLL NKKAEPSFVE SLCQKMNELN QEISKEATIL GK GFRIGHS YFCCGLEDGT SPDTQWLNEI VMTDIAPLLE EYFFDDPYKQ QKWTNKLLGD SSGSHHHHHH UniProtKB: Type IV methyl-directed restriction enzyme EcoKMcrB subunit |
-Macromolecule #2: Protein McrC
Macromolecule | Name: Protein McrC / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 40.643625 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MEQPVIPVRN IYYMLTYAWG YLQEIKQANL EAIPGNNLLD ILGYVLNKGV LQLSRRGLEL DYNPNTEIIP GIKGRIEFAK TIRGFHLNH GKTVSTFDML NEDTLANRII KSTLAILIKH EKLNSTIRDE ARSLYRKLPG ISTLHLTPQH FSYLNGGKNT R YYKFVISV ...String: MEQPVIPVRN IYYMLTYAWG YLQEIKQANL EAIPGNNLLD ILGYVLNKGV LQLSRRGLEL DYNPNTEIIP GIKGRIEFAK TIRGFHLNH GKTVSTFDML NEDTLANRII KSTLAILIKH EKLNSTIRDE ARSLYRKLPG ISTLHLTPQH FSYLNGGKNT R YYKFVISV CKFIVNNSIP GQNKGHYRFY DFERNEKEMS LLYQKFLYEF CRRELTSANT TRSYLKWDAS SISDQSLNLL PR METDITI RSSEKILIVD AKYYKSIFSR RMGTEKFHSQ NLYQLMNYLW SLKPENGENI GGLLIYPHVD TAVKHRYKIN GFD IGLCTV NLGQEWPCIH QELLDIFDEY LK UniProtKB: Type IV methyl-directed restriction enzyme EcoKMcrBC |
-Macromolecule #3: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
Macromolecule | Name: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / type: ligand / ID: 3 / Number of copies: 6 / Formula: GNP |
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Molecular weight | Theoretical: 522.196 Da |
Chemical component information | ![]() ChemComp-GNP: |
-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 |
-Macromolecule #5: GUANOSINE-5'-DIPHOSPHATE
Macromolecule | Name: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 6 / Formula: GDP |
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Molecular weight | Theoretical: 443.201 Da |
Chemical component information | ![]() ChemComp-GDP: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 4.0 mg/mL | |||||||||||||||
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Buffer | pH: 7.4 Component:
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Grid | Model: C-flat-2/2 4C / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 2-20 / Number grids imaged: 1 / Number real images: 3326 / Average exposure time: 8.0 sec. / Average electron dose: 1.5 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Calibrated defocus max: 5.0 µm / Calibrated defocus min: 0.3 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal magnification: 130000 |
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: AB INITIO MODEL / Overall B value: 74 / Target criteria: Cross-correlation coefficient |
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Output model | ![]() PDB-6hz6: |