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Open data
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Basic information
| Entry | Database: PDB / ID: 9lxh | ||||||||||||||||||||||||
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| Title | DOCK5/ELMO1 complex with RhoG and Rac1 on lipid membrane | ||||||||||||||||||||||||
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Keywords | SIGNALING PROTEIN / Complex / Rho-GTPase / GEF / Lipid membrane | ||||||||||||||||||||||||
| Function / homology | Function and homology informationregulation of ruffle assembly / negative regulation of vascular associated smooth muscle contraction / podosome assembly / cortical cytoskeleton organization / guanyl-nucleotide exchange factor complex / activation of GTPase activity / bone remodeling / myoblast fusion / Nef and signal transduction / positive regulation of vascular associated smooth muscle cell migration ...regulation of ruffle assembly / negative regulation of vascular associated smooth muscle contraction / podosome assembly / cortical cytoskeleton organization / guanyl-nucleotide exchange factor complex / activation of GTPase activity / bone remodeling / myoblast fusion / Nef and signal transduction / positive regulation of vascular associated smooth muscle cell migration / RHO GTPases activate KTN1 / podosome / anchoring junction / phagocytosis, engulfment / establishment or maintenance of cell polarity / Rac protein signal transduction / positive regulation of epithelial cell migration / regulation of postsynapse assembly / RHOG GTPase cycle / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / GPVI-mediated activation cascade / Rho protein signal transduction / RAC1 GTPase cycle / positive regulation of substrate adhesion-dependent cell spreading / GTPase activator activity / secretory granule membrane / actin filament organization / guanyl-nucleotide exchange factor activity / cell chemotaxis / regulation of actin cytoskeleton organization / positive regulation of protein localization to plasma membrane / cell projection / FCGR3A-mediated phagocytosis / cell motility / Regulation of actin dynamics for phagocytic cup formation / SH3 domain binding / small GTPase binding / VEGFA-VEGFR2 Pathway / Constitutive Signaling by Aberrant PI3K in Cancer / cell migration / PIP3 activates AKT signaling / regulation of cell shape / Factors involved in megakaryocyte development and platelet production / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / actin cytoskeleton organization / cytoplasmic vesicle / cytoskeleton / postsynapse / focal adhesion / GTPase activity / positive regulation of cell population proliferation / apoptotic process / Neutrophil degranulation / protein kinase binding / endoplasmic reticulum membrane / positive regulation of DNA-templated transcription / GTP binding / glutamatergic synapse / extracellular exosome / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.52 Å | ||||||||||||||||||||||||
Authors | Shinoda, T. / Katsura, K. / Kukimoto-Niino, M. / Shirouzu, M. | ||||||||||||||||||||||||
| Funding support | Japan, 1items
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Citation | Journal: To Be PublishedTitle: Conformational alteration of DOCK5-ELMO1 signalosome on lipid membrane Authors: Shinoda, T. / Katsura, K. / Ishizuka-Katsura, Y. / Hanada, K. / Yonemochi, M. / Miyamoto, Y. / Kukimoto-Niino, M. / Yamauchi, J. / Shirouzu, M. | ||||||||||||||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9lxh.cif.gz | 421.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9lxh.ent.gz | 328.4 KB | Display | PDB format |
| PDBx/mmJSON format | 9lxh.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9lxh_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9lxh_full_validation.pdf.gz | 1.5 MB | Display | |
| Data in XML | 9lxh_validation.xml.gz | 76.8 KB | Display | |
| Data in CIF | 9lxh_validation.cif.gz | 114.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lx/9lxh ftp://data.pdbj.org/pub/pdb/validation_reports/lx/9lxh | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 63477MC ![]() 9lx0C C: citing same article ( M: map data used to model this data |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 84379.797 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELMO1, KIAA0281 / Production host: Homo sapiens (human) / References: UniProt: Q92556 |
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| #2: Protein | Mass: 216022.406 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DOCK5 / Production host: Homo sapiens (human) / References: UniProt: Q9H7D0 |
| #3: Protein | Mass: 23692.918 Da / Num. of mol.: 1 / Mutation: Q61L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RHOG, ARHG / Production host: ![]() |
| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: DOCK5/ELMO1 complex with RhoG and Rac1 on lipid membrane Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| 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 / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
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| 3D reconstruction | Resolution: 7.52 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 55365 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 7.52 Å / Cross valid method: NONE Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
Japan, 1items
Citation


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FIELD EMISSION GUN