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Open data
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Basic information
Entry | Database: PDB / ID: 6uka | ||||||
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Title | Crystal structure of RHOG and ELMO complex | ||||||
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![]() | SIGNALING PROTEIN / RHOG / ELMO / RBD / complex / CELL ADHESION | ||||||
Function / homology | ![]() small GTPase binding => GO:0031267 / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / regulation of ruffle assembly / Regulation of actin dynamics for phagocytic cup formation / engulfment of apoptotic cell / cortical cytoskeleton organization / VEGFA-VEGFR2 Pathway / activation of GTPase activity / RHO GTPases activate KTN1 / motor neuron axon guidance ...small GTPase binding => GO:0031267 / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / regulation of ruffle assembly / Regulation of actin dynamics for phagocytic cup formation / engulfment of apoptotic cell / cortical cytoskeleton organization / VEGFA-VEGFR2 Pathway / activation of GTPase activity / RHO GTPases activate KTN1 / motor neuron axon guidance / establishment or maintenance of cell polarity / Rac protein signal transduction / Rho protein signal transduction / RHOG GTPase cycle / phagocytosis / GPVI-mediated activation cascade / cell chemotaxis / secretory granule membrane / cell projection / cell motility / regulation of actin cytoskeleton organization / positive regulation of protein localization to plasma membrane / actin filament organization / receptor tyrosine kinase binding / cell-cell adhesion / SH3 domain binding / Constitutive Signaling by Aberrant PI3K in Cancer / PIP3 activates AKT signaling / regulation of cell shape / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / cytoplasmic vesicle / actin cytoskeleton organization / cytoskeleton / focal adhesion / GTPase activity / apoptotic process / positive regulation of cell population proliferation / Neutrophil degranulation / endoplasmic reticulum membrane / GTP binding / protein kinase binding / positive regulation of DNA-templated transcription / extracellular exosome / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Jo, C.H. / Killoran, R.C. / Smith, M.J. | ||||||
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![]() | ![]() Title: Structure of the DOCK2-ELMO1 complex provides insights into regulation of the auto-inhibited state. Authors: Leifu Chang / Jing Yang / Chang Hwa Jo / Andreas Boland / Ziguo Zhang / Stephen H McLaughlin / Afnan Abu-Thuraia / Ryan C Killoran / Matthew J Smith / Jean-Francois Côté / David Barford / ![]() ![]() ![]() ![]() Abstract: DOCK (dedicator of cytokinesis) proteins are multidomain guanine nucleotide exchange factors (GEFs) for RHO GTPases that regulate intracellular actin dynamics. DOCK proteins share catalytic (DOCK) ...DOCK (dedicator of cytokinesis) proteins are multidomain guanine nucleotide exchange factors (GEFs) for RHO GTPases that regulate intracellular actin dynamics. DOCK proteins share catalytic (DOCK) and membrane-associated (DOCK) domains. The structurally-related DOCK1 and DOCK2 GEFs are specific for RAC, and require ELMO (engulfment and cell motility) proteins for function. The N-terminal RAS-binding domain (RBD) of ELMO (ELMO) interacts with RHOG to modulate DOCK1/2 activity. Here, we determine the cryo-EM structures of DOCK2-ELMO1 alone, and as a ternary complex with RAC1, together with the crystal structure of a RHOG-ELMO2 complex. The binary DOCK2-ELMO1 complex adopts a closed, auto-inhibited conformation. Relief of auto-inhibition to an active, open state, due to a conformational change of the ELMO1 subunit, exposes binding sites for RAC1 on DOCK2, and RHOG and BAI GPCRs on ELMO1. Our structure explains how up-stream effectors, including DOCK2 and ELMO1 phosphorylation, destabilise the auto-inhibited state to promote an active GEF. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83.1 KB | Display | ![]() |
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PDB format | ![]() | 48.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 340.2 KB | Display | ![]() |
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Full document | ![]() | 341 KB | Display | |
Data in XML | ![]() | 1.9 KB | Display | |
Data in CIF | ![]() | 5.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6tgbC ![]() 6tgcC ![]() 1a2bS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 21334.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 9032.248 Da / Num. of mol.: 1 / Fragment: Ras-binding Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Chemical | ChemComp-GNP / |
#4: Chemical | ChemComp-MG / |
#5: Water | ChemComp-HOH / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 42.08 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: 0.1M CHES, 0.95M sodium citrate / PH range: 8.5 - 9.0 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SEALED TUBE / Type: BRUKER D8 QUEST / Wavelength: 1.34165 Å |
Detector | Type: Bruker PHOTON II / Detector: PIXEL / Date: Nov 9, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.34165 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→27.01 Å / Num. obs: 38996 / % possible obs: 93.9 % / Redundancy: 5.7 % / Biso Wilson estimate: 17.88 Å2 / Rmerge(I) obs: 0.1131 / Net I/σ(I): 13.42 |
Reflection shell | Resolution: 2.4→2.44 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.2591 / Mean I/σ(I) obs: 5.4 / Num. unique obs: 466 / % possible all: 89.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1A2B Resolution: 2.4→27.01 Å / SU ML: 0.2833 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.4928
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.54 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→27.01 Å
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Refine LS restraints |
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LS refinement shell |
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