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Yorodumi- EMDB-36454: Cryo-EM structure of a Legionella effector complexed with actin a... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-36454 | |||||||||||||||
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Title | Cryo-EM structure of a Legionella effector complexed with actin and AMP | |||||||||||||||
Map data | ||||||||||||||||
Sample |
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Keywords | AMPylation / TOXIN | |||||||||||||||
Function / homology | Function and homology information cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / actin filament bundle / filamentous actin / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament ...cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / actin filament bundle / filamentous actin / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / actin filament polymerization / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / lamellipodium / cell body / hydrolase activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / magnesium ion binding / ATP binding / identical protein binding / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | Legionella sainthelensi (bacteria) / Oryctolagus cuniculus (rabbit) | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.66 Å | |||||||||||||||
Authors | Zhou XT / Wang XF / Tan JX / Zhu YQ | |||||||||||||||
Funding support | China, 4 items
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Citation | Journal: To Be Published Title: Cryo-EM structure of a Legionella effector complexed with actin and AMP Authors: Zhou XT / Wang XF / Tan JX / Zhu YQ | |||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_36454.map.gz | 59.8 MB | EMDB map data format | |
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Header (meta data) | emd-36454-v30.xml emd-36454.xml | 16.7 KB 16.7 KB | Display Display | EMDB header |
Images | emd_36454.png | 67.3 KB | ||
Filedesc metadata | emd-36454.cif.gz | 6.4 KB | ||
Others | emd_36454_half_map_1.map.gz emd_36454_half_map_2.map.gz | 59.4 MB 59.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-36454 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-36454 | HTTPS FTP |
-Related structure data
Related structure data | 8jo3MC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_36454.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 0.93 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_36454_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_36454_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Cryo-EM structure of a Legionella effector complexed with actin a...
Entire | Name: Cryo-EM structure of a Legionella effector complexed with actin and AMP |
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Components |
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-Supramolecule #1: Cryo-EM structure of a Legionella effector complexed with actin a...
Supramolecule | Name: Cryo-EM structure of a Legionella effector complexed with actin and AMP type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Legionella sainthelensi (bacteria) |
-Macromolecule #1: Substrate of the Dot/Icm secretion system
Macromolecule | Name: Substrate of the Dot/Icm secretion system / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Legionella sainthelensi (bacteria) |
Molecular weight | Theoretical: 50.62148 KDa |
Recombinant expression | Organism: Escherichia coli BL21 (bacteria) |
Sequence | String: MSYTKIESSL LLALDYPKLD ESDFILLLTK FLEKKLGNND NYPTFSKQIQ KYYLEQEYKK AIENILRLCQ ENETLLGTNL VQRLITKSS QVTSNPKDNE SRRFYEVLYA EHLESILRKD FDCSIFDELN EAYNEVRPEY TVNDLTKINT FEEARKLILA F VMLNDNVE ...String: MSYTKIESSL LLALDYPKLD ESDFILLLTK FLEKKLGNND NYPTFSKQIQ KYYLEQEYKK AIENILRLCQ ENETLLGTNL VQRLITKSS QVTSNPKDNE SRRFYEVLYA EHLESILRKD FDCSIFDELN EAYNEVRPEY TVNDLTKINT FEEARKLILA F VMLNDNVE LGLKAQSAIY QKKDRSREEL GQVLTANPGI MKPNSPNFAD NTVPIKKIDK IAIDEKKAGG YSKTNPQVPF VA SLSGTTY SLVVVLQKYM DKHKTDPNLE KKINNIVMLW TSAYIKDGYH SYKEVIDIFK DAHIQSIFAR ANIKLDYAII DDT DHEFHR AQEYTQGIAT KAMMHQELVQ KVQEKSMREE KQKQMLLFCG VLVNQLNQDP KSKEKYPEQL ESLNALYKNW NAGT IKNQE FKKECTQVCT EIQIKEQNTP SSGWSHPQFE K UniProtKB: Substrate of the Dot/Icm secretion system |
-Macromolecule #2: Actin, alpha skeletal muscle
Macromolecule | Name: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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Source (natural) | Organism: Oryctolagus cuniculus (rabbit) |
Molecular weight | Theoretical: 42.096953 KDa |
Sequence | String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLDSGD G VTHNVPIY ...String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLDSGD G VTHNVPIY EGYALPHAIM RLDLAGRDLT DYLMKILTER GYSFVTTAER EIVRDIKEKL CYVALDFENE MATAASSSSL EK SYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVMSGGTTM YPGIADRMQK EIT ALAPST MKIKIIAPPE RKYSVWIGGS ILASLSTFQQ MWITKQEYDE AGPSIVHRKC F UniProtKB: Actin, alpha skeletal muscle |
-Macromolecule #3: ADENOSINE MONOPHOSPHATE
Macromolecule | Name: ADENOSINE MONOPHOSPHATE / type: ligand / ID: 3 / Number of copies: 1 / Formula: AMP |
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Molecular weight | Theoretical: 347.221 Da |
Chemical component information | ChemComp-AMP: |
-Macromolecule #4: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Macromolecule #5: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 1 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ChemComp-ATP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Grid | Model: Quantifoil R0.6/1 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 180 sec. |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.8 µm |
Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.66 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 868128 |
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo built model |
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Output model | PDB-8jo3: |