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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-10404 | |||||||||
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Title | FtsK motor domain bound to dsDNA, ADP-state | |||||||||
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Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.63 Å | |||||||||
![]() | Jean NL / Lowe J | |||||||||
Funding support | ![]()
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![]() | ![]() Title: FtsK in motion reveals its mechanism for double-stranded DNA translocation. Authors: Nicolas L Jean / Trevor J Rutherford / Jan Löwe / ![]() Abstract: FtsK protein contains a fast DNA motor that is involved in bacterial chromosome dimer resolution. During cell division, FtsK translocates double-stranded DNA until both recombination sites are ...FtsK protein contains a fast DNA motor that is involved in bacterial chromosome dimer resolution. During cell division, FtsK translocates double-stranded DNA until both recombination sites are placed at mid cell for subsequent dimer resolution. Here, we solved the 3.6-Å resolution electron cryo-microscopy structure of the motor domain of FtsK while translocating on its DNA substrate. Each subunit of the homo-hexameric ring adopts a unique conformation and one of three nucleotide states. Two DNA-binding loops within four subunits form a pair of spiral staircases within the ring, interacting with the two DNA strands. This suggests that simultaneous conformational changes in all ATPase domains at each catalytic step generate movement through a mechanism related to filament treadmilling. While the ring is only rotating around the DNA slowly, it is instead the conformational states that rotate around the ring as the DNA substrate is pushed through. #1: ![]() Title: FtsK in motion reveals its mechanism for double-stranded DNA translocation Authors: Jean NL / Rutherford TJ / Lowe J | |||||||||
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 | ![]() | 4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.5 KB 15.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 7.6 KB | Display | ![]() |
Images | ![]() | 150.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 251.3 KB | Display | ![]() |
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Full document | ![]() | 250.4 KB | Display | |
Data in XML | ![]() | 10 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : FtsK motor domain bound to dsDNA, ADP-state
Entire | Name: FtsK motor domain bound to dsDNA, ADP-state |
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Components |
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-Supramolecule #1: FtsK motor domain bound to dsDNA, ADP-state
Supramolecule | Name: FtsK motor domain bound to dsDNA, ADP-state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #2: FtsK motor domain
Supramolecule | Name: FtsK motor domain / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Supramolecule #3: DNA
Supramolecule | Name: DNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: synthetic construct (others) |
Recombinant expression | Organism: synthetic construct (others) |
-Macromolecule #1: DNA translocase FtsK
Macromolecule | Name: DNA translocase FtsK / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MVPDRREQSK AKERLLEREE ALAKHMSERE KRPPPKIDPP PSPKAPEPSK RVLKEKQAPL FVDTAVEGTL PPLSLLDPAE VKQKSYSPES LEAMSRLLEI KLKEFGVEVS VDSVHPGPVI TRFEIQPAAG VKVSRISNLA KDLARSLAVI SVRVVEVIPG KTTVGIEIPN ...String: MVPDRREQSK AKERLLEREE ALAKHMSERE KRPPPKIDPP PSPKAPEPSK RVLKEKQAPL FVDTAVEGTL PPLSLLDPAE VKQKSYSPES LEAMSRLLEI KLKEFGVEVS VDSVHPGPVI TRFEIQPAAG VKVSRISNLA KDLARSLAVI SVRVVEVIPG KTTVGIEIPN EDRQMVRFSE VLSSPEYDEH KSTVPLALGH DIGGRPIITD LAKMPHLLVA GTTGSGKSVG VNAMLLSILF KSTPSEARLI MIDPKMLELS IYEGIPHLLC PVVTDMKEAA NALRWSVAEM ERRYRLMAAM GVRNLAGFNR KVKDAEEAGT PLTDPLFRRE SPDDEPPQLS TLPTIVVVVD EFADMMMIVG KKVEELIARI AQKARAAGIH LILATQRPSV DVITGLIKAN IPTRIAFQVS SKIDSRTILD QGGAEQLLGH GDMLYLPPGT GLPIRVHGAF VSDDEVHRVV EAWKLRGAPD YIEDILAGVD EGGKLHHHHH H |
-Macromolecule #2: dsDNA substrate
Macromolecule | Name: dsDNA substrate / type: dna / ID: 2 / Classification: DNA |
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Source (natural) | Organism: unidentified (others) |
Sequence | String: ATATATATAT ATATATATAT |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 / Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE | ||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV | ||||||||
Details | 0.7 m/mL FtsK 1.5 uM 45 bp DNA |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number real images: 771 / Average electron dose: 39.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |