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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Structure of V.cholera DdmDE (2D:1E) in complex with DNA | |||||||||
Map data | Structure of V.cholera DdmDE (2D:1E) in complex with DNA | |||||||||
Sample |
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Keywords | DNA defense modules (Ddm) / DdmDE / anti-plasmid / bacterial immune system / IMMUNE SYSTEM-DNA complex | |||||||||
| Function / homology | Uncharacterized protein / Helicase/UvrB N-terminal domain-containing protein Function and homology information | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.28 Å | |||||||||
Authors | Shen ZF / Yang XY / Fu TM | |||||||||
| Funding support | 1 items
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Citation | Journal: Cell / Year: 2024Title: DdmDE eliminates plasmid invasion by DNA-guided DNA targeting. Authors: Xiao-Yuan Yang / Zhangfei Shen / Chen Wang / Kotaro Nakanishi / Tian-Min Fu / ![]() Abstract: Horizontal gene transfer is a key driver of bacterial evolution, but it also presents severe risks to bacteria by introducing invasive mobile genetic elements. To counter these threats, bacteria have ...Horizontal gene transfer is a key driver of bacterial evolution, but it also presents severe risks to bacteria by introducing invasive mobile genetic elements. To counter these threats, bacteria have developed various defense systems, including prokaryotic Argonautes (pAgos) and the DNA defense module DdmDE system. Through biochemical analysis, structural determination, and in vivo plasmid clearance assays, we elucidate the assembly and activation mechanisms of DdmDE, which eliminates small, multicopy plasmids. We demonstrate that DdmE, a pAgo-like protein, acts as a catalytically inactive, DNA-guided, DNA-targeting defense module. In the presence of guide DNA, DdmE targets plasmids and recruits a dimeric DdmD, which contains nuclease and helicase domains. Upon binding to DNA substrates, DdmD transitions from an autoinhibited dimer to an active monomer, which then translocates along and cleaves the plasmids. Together, our findings reveal the intricate mechanisms underlying DdmDE-mediated plasmid clearance, offering fundamental insights into bacterial defense systems against plasmid invasions. | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_44516.map.gz | 54.7 MB | EMDB map data format | |
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| Header (meta data) | emd-44516-v30.xml emd-44516.xml | 17.4 KB 17.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_44516_fsc.xml | 11.8 KB | Display | FSC data file |
| Images | emd_44516.png | 141 KB | ||
| Filedesc metadata | emd-44516.cif.gz | 7.2 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-44516 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-44516 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9bgkMC ![]() 9bf1C ![]() 9bf5C ![]() 9c6qC C: citing same article ( M: atomic model generated by this map |
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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_44516.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Structure of V.cholera DdmDE (2D:1E) in complex with DNA | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.11 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : DdmD dimer bind DdmE in complex with DNA
| Entire | Name: DdmD dimer bind DdmE in complex with DNA |
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| Components |
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-Supramolecule #1: DdmD dimer bind DdmE in complex with DNA
| Supramolecule | Name: DdmD dimer bind DdmE in complex with DNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: guide DNA
| Macromolecule | Name: guide DNA / type: dna / ID: 1 / Number of copies: 1 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 3.767465 KDa |
| Sequence | String: (DA)(DG)(DG)(DT)(DG)(DA)(DG)(DG)(DA)(DG) (DT)(DC) |
-Macromolecule #2: complementary target DNA
| Macromolecule | Name: complementary target DNA / type: dna / ID: 2 / Number of copies: 1 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 7.594898 KDa |
| Sequence | String: (DA)(DT)(DG)(DG)(DA)(DC)(DT)(DC)(DC)(DT) (DC)(DA)(DC)(DC)(DT)(DG)(DC)(DA)(DG)(DG) (DT)(DT)(DC)(DA)(DC) |
-Macromolecule #3: non-complementary target DNA (long)
| Macromolecule | Name: non-complementary target DNA (long) / type: dna / ID: 3 / Number of copies: 1 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 8.093215 KDa |
| Sequence | String: (DG)(DT)(DG)(DA)(DA)(DC)(DC)(DT)(DG)(DC) (DA)(DG)(DG)(DT)(DG)(DA)(DG)(DG)(DA)(DG) (DT)(DC)(DC)(DA)(DT)(DG) |
-Macromolecule #4: non-complementary target DNA (short)
| Macromolecule | Name: non-complementary target DNA (short) / type: dna / ID: 4 / Number of copies: 1 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 3.702428 KDa |
| Sequence | String: (DT)(DG)(DA)(DG)(DG)(DA)(DG)(DT)(DC)(DC) (DA)(DT) |
-Macromolecule #5: DdmE
| Macromolecule | Name: DdmE / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 79.195891 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MVTPQLEPSS QGPLSTLIEQ ISIDTDWVDR SFAIYCVSYK GIDFSERPKR LVTLASETYK SGSVYCLVKG ANKEACYWVL LPKDSKLDL KDTSLAIKPS SAAELPTWQL ARLLIKAIPK VLSGTMPEIK RFESEGLYYL VKSKKLPKDH SGYELTTVEI D LAPCAALG ...String: MVTPQLEPSS QGPLSTLIEQ ISIDTDWVDR SFAIYCVSYK GIDFSERPKR LVTLASETYK SGSVYCLVKG ANKEACYWVL LPKDSKLDL KDTSLAIKPS SAAELPTWQL ARLLIKAIPK VLSGTMPEIK RFESEGLYYL VKSKKLPKDH SGYELTTVEI D LAPCAALG FKQTLSMGTK TFSPLSWFTL ENGEVQKKAR FATRYQLDDV GKLVSKSIKG DYIKKPLYSN AKNRIQAIDI TK ESYSGFQ LSKVGILEQF MQDLKQAYGD SVSVKLQRIP GEKHRFVSDT IVKNHYVGLF DALKEHRLVI CDLTENQDTD AAL TLLHGI EHLDINAEIA EVPIRGALNI LIVGNKDTYK SDEEDPYQVY RKKYQDTVFQ SCYPERLWNR QGQPNRHVVE VLLK ELLIK LEVHTRKHLI EYPSGPERCV YYMPQRPKDE SSEVRDEPWP VYASKLVGDE WQYTQATQEE LEDIELDLGN DKRHV FHGF ERSPVIYWPE TGDYAIFIDT GIQMLPEFEA VAERLRELKE GRSQDVPIAL LAQFIEENPE SKVINKLRAI LSEWDD VAP LPFDEFSTIA YKSSDEKQFY DWLREQGFFL KTSIRGQSEG FFNASLGFFY NREQGMYFAG GKGSPQSKIE TFSHLYL IK HSFDALPEEV ENLFDVYHLR HRLPTVTPYP FKHLREYVEM QRFRS UniProtKB: Uncharacterized protein |
-Macromolecule #6: Helicase/UvrB N-terminal domain-containing protein
| Macromolecule | Name: Helicase/UvrB N-terminal domain-containing protein / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 136.155328 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MNVSIEEFTH FDFQLVPEPS PLDLVITEPL KNHIEVNGVK SGALLPLPFQ TGIGKTYTAL NFLLQQMLEQ VRSELKEENT GKKSKRLLY YVTDSVDNVV SAKADLLKLI EKQTVKGEPR FTLEQQEYLK AQIVHLPNQS EQLLQCSDAV LNDVLIGFNL N AERDVQAE ...String: MNVSIEEFTH FDFQLVPEPS PLDLVITEPL KNHIEVNGVK SGALLPLPFQ TGIGKTYTAL NFLLQQMLEQ VRSELKEENT GKKSKRLLY YVTDSVDNVV SAKADLLKLI EKQTVKGEPR FTLEQQEYLK AQIVHLPNQS EQLLQCSDAV LNDVLIGFNL N AERDVQAE WSAISGLRRH ASNPEVKISL NRQAGYFYRN LIDRLQKKQK GADRVLLSGS LLASVETLLP GEKIRNGSAH VA FLTTSKF LKGFHNTRSR YSPLRDLSGA VLIIDEIDKQ NQVILSELCK QQAQDLIWAI RTLRANFRDH QLESSPRYDK IED LFEPLR ERLEEFGTNW NLAFAFNTEG ANLNERPVRL FSDRSFTHVS SATHKLSLKS DFLRRKNLIF SDEKVEGSLI EKHG LLTRF VNEADVIYQW FLGTMRKAVF QYWENVRGLE IEVRENRSLE GTFQEAVQSL LTHFNLQEFE SAVYESFDTR GLRQS AGGK ANKLSSSKSY HHTGLKLVEV AHNQGTRDTV NCKASFLNTS PSGVLADMVD AGAVILGISA TARADTVIHN FDFKYL NER LGNKLLSLSR EQKQRVNNYY HSRRNYKDNG VVLTVKYLNS RDAFLDALLE EYKPEARSSH FILNHYLGIA ESEQAFV RS WLSKLLASIK AFISSPDNRY MLSLLNRTLD TTRQNINDFI QFCCDKWAKE FNVKTKTFFG VNADWMRLVG YDEISKHL N TELGKVVVFS TYASMGAGKN PDYAVNLALE GESLISVADV TYSTQLRSDI DSIYLEKPTQ LLLSDDYSHT ANQLCQFHQ ILSLQENGEL SPKSAENWCR QQLMGMSRER SLQQYHQTSD YQSAVRKYIE QAVGRAGRTS LKRKQILLFV DSGLKEILAE ESRDPSLFS HEYVALVNKA KSAGKSIVED RAVRRLFNLA QRNNKDGMLS IKALVHRLHN QPASKSDIQE WQDIRTQLLR Y PTVAFQPE RFNRLYLQSM TKGYYRYQGN LDGDPNSFEF FDRVPYGDMV SEEDCSLATL VQNQYVRPWF ERKGFACSWQ KE ANVMTPI MFTNIYKGAL GEQAVEAVLT AFDFTFEEVP NSIYERFDNR VIFAGIEQPI WLDSKYWKHE GNESSEGYSS KIA LVEEEF GPSKFIYVNA LGDTSKPIRY LNSCFVETSP QLAKVIEIPA LIDDSNADTN RTAVQELIKW LHHS UniProtKB: Helicase/UvrB N-terminal domain-containing protein |
-Macromolecule #7: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 7 / Number of copies: 1 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-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: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 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: 2.5 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Processing
FIELD EMISSION GUN

