|Entry||Database: PDB / ID: 1.0E+96 |
|Title||Structure of the Rac/p67phox complex|
|Keywords||SIGNALING PROTEIN / SIGNALLING COMPLEX / GTPASE / NADPH OXIDASE / PROTEIN-PROTEIN COMPLEX / TPR MOTIF|
|Function / homology|
Function and homology information
superoxide-generating NAD(P)H oxidase activity / phagolysosome / superoxide-generating NADPH oxidase activator activity / regulation of respiratory burst / regulation of neutrophil migration / negative regulation of interleukin-23 production / localization within membrane / Activated NTRK2 signals through CDK5 / Cross-presentation of particulate exogenous antigens (phagosomes) / NADPH oxidase complex ...superoxide-generating NAD(P)H oxidase activity / phagolysosome / superoxide-generating NADPH oxidase activator activity / regulation of respiratory burst / regulation of neutrophil migration / negative regulation of interleukin-23 production / localization within membrane / Activated NTRK2 signals through CDK5 / Cross-presentation of particulate exogenous antigens (phagosomes) / NADPH oxidase complex / negative regulation of receptor-mediated endocytosis / engulfment of apoptotic cell / regulation of hydrogen peroxide metabolic process / ruffle assembly / NTRK2 activates RAC1 / Rho GDP-dissociation inhibitor binding / Inactivation of CDC42 and RAC1 / WNT5:FZD7-mediated leishmania damping / respiratory burst / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / PCP/CE pathway / cell projection assembly / RHO GTPases activate CIT / RHO GTPases activate KTN1 / ROS and RNS production in phagocytes / cortical cytoskeleton organization / ruffle organization / hepatocyte growth factor receptor signaling pathway / positive regulation of neutrophil chemotaxis / superoxide anion generation / Azathioprine ADME / regulation of stress fiber assembly / negative regulation of fibroblast migration / sphingosine-1-phosphate receptor signaling pathway / thioesterase binding / regulation of nitric oxide biosynthetic process / Wnt signaling pathway, planar cell polarity pathway / regulation of lamellipodium assembly / Nef and signal transduction / motor neuron axon guidance / Sema4D mediated inhibition of cell attachment and migration / Activation of RAC1 / positive regulation of Rho protein signal transduction / Ephrin signaling / positive regulation of cell-substrate adhesion / MET activates RAP1 and RAC1 / DCC mediated attractive signaling / CD28 dependent Vav1 pathway / lamellipodium assembly / Activation of RAC1 downstream of NMDARs / semaphorin-plexin signaling pathway / NRAGE signals death through JNK / regulation of cell size / Rac protein signal transduction / DSCAM interactions / superoxide metabolic process / positive regulation of lamellipodium assembly / establishment or maintenance of cell polarity / small GTPase mediated signal transduction / Detoxification of Reactive Oxygen Species / RHO GTPases activate PAKs / ficolin-1-rich granule membrane / positive regulation of focal adhesion assembly / Sema3A PAK dependent Axon repulsion / EPH-ephrin mediated repulsion of cells / RHO GTPases activate IQGAPs / anatomical structure morphogenesis / RAC3 GTPase cycle / RAC2 GTPase cycle / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / RHO GTPases Activate WASPs and WAVEs / RHO GTPases Activate NADPH Oxidases / RHO GTPases activate PKNs / phagocytosis / cellular defense response / localization / regulation of actin cytoskeleton organization / GPVI-mediated activation cascade / EPHB-mediated forward signaling / positive regulation of microtubule polymerization / G protein activity / positive regulation of stress fiber assembly / positive regulation of substrate adhesion-dependent cell spreading / regulation of cell migration / RAC1 GTPase cycle / neuron migration / acrosomal vesicle / actin filament polymerization / small monomeric GTPase / cell motility / actin filament organization / cell-matrix adhesion / substrate adhesion-dependent cell spreading / secretory granule membrane / RHO GTPases Activate Formins / VEGFR2 mediated vascular permeability / Translocation of SLC2A4 (GLUT4) to the plasma membrane / positive regulation of endothelial cell migration / Signal transduction by L1 / cell projection
Similarity search - Function
Neutrophil cytosol factor 2, PB1 domain / Neutrophil cytosol factor 2 / Neutrophil cytosol factor 2, SH3 domain 1 / PB1 domain / PB1 domain / PB1 domain profile. / PB1 domain / small GTPase Rho family profile. / Small GTPase Rho / Tetratricopeptide repeat domain ...Neutrophil cytosol factor 2, PB1 domain / Neutrophil cytosol factor 2 / Neutrophil cytosol factor 2, SH3 domain 1 / PB1 domain / PB1 domain / PB1 domain profile. / PB1 domain / small GTPase Rho family profile. / Small GTPase Rho / Tetratricopeptide repeat domain / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Rho (Ras homology) subfamily of Ras-like small GTPases / Small GTPase / Ras family / SH3 domain / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Small GTP-binding protein domain / Tetratricopeptide-like helical domain superfamily / Alpha Horseshoe / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / Ras-related C3 botulinum toxin substrate 1 / Neutrophil cytosol factor 2 / Ras-related C3 botulinum toxin substrate 1
Similarity search - Component
|Biological species||HOMO SAPIENS (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å|
|Authors||Lapouge, K. / Smith, S.J.M. / Walker, P.A. / Gamblin, S.J. / Smerdon, S.J. / Rittinger, K.|
|Citation||Journal: Mol.Cell / Year: 2000|
Title: Structure of the TPR domain of p67phox in complex with Rac.GTP.
Authors: Lapouge, K. / Smith, S.J. / Walker, P.A. / Gamblin, S.J. / Smerdon, S.J. / Rittinger, K.
|Structure viewer||Molecule: |
Downloads & links
A: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1
B: NEUTROPHIL CYTOSOL FACTOR 2 (NCF-2) TPR DOMAIN, RESIDUES 1-203
|#1: Protein|| |
Mass: 21429.062 Da / Num. of mol.: 1 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX-2T / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P15154, UniProt: P63000*PLUS
|#2: Protein|| |
Mass: 23490.471 Da / Num. of mol.: 1 / Fragment: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX-4T / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P19878
|#3: Chemical|| ChemComp-GTP / |
|#4: Chemical|| ChemComp-MG / |
|#5: Water|| ChemComp-HOH / |
|Compound details||CHAIN A ENGINEERED MUTATION MET1PRO, GLN61LEU RAC1 ARE GTP-BINDING PROTEINS ASSOCIATED WITH PLASMA ...CHAIN A ENGINEERED|
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 3.08 Å3/Da / Density % sol: 54.6 %|
|Crystal grow||pH: 10.5 |
Details: 0.1 M CAPS PH 10.5, 0.2 M LI ACETATE, 0.8 M NAH2PO4, 1.2 M K2HPO4
*PLUSTemperature: 18 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop
|Components of the solutions|
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: SRS / Beamline: PX7.2 / Wavelength: 1.488|
|Detector||Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 2000|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.488 Å / Relative weight: 1|
|Reflection||Resolution: 2.4→15 Å / Num. obs: 123873 / % possible obs: 94 % / Redundancy: 5.9 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 16.9|
|Reflection shell||Resolution: 2.4→2.45 Å / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 4.2 / % possible all: 100|
*PLUSNum. obs: 20975 / Num. measured all: 123873
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: 1MH1, 1A17
Resolution: 2.4→15 Å / SU ML: 0.189 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.411 / ESU R Free: 0.288
|Displacement parameters||Biso mean: 29.7 Å2|
|Refinement step||Cycle: LAST / Resolution: 2.4→15 Å|
|Refine LS restraints|
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