+Open data
-Basic information
Entry | Database: PDB / ID: 5f5p | ||||||
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Title | Molecular Basis for Shroom2 Recognition by Rock1 | ||||||
Components |
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Keywords | PROTEIN BINDING / coiled-coil / complex / cytoskeleton / kinase | ||||||
Function / homology | Function and homology information eye pigment granule organization / establishment of melanosome localization / cellular pigment accumulation / regulation of amyloid-beta formation / regulation of angiotensin-activated signaling pathway / apical constriction / Rho-dependent protein serine/threonine kinase activity / podocyte cell migration / ligand-gated sodium channel activity / regulation of keratinocyte differentiation ...eye pigment granule organization / establishment of melanosome localization / cellular pigment accumulation / regulation of amyloid-beta formation / regulation of angiotensin-activated signaling pathway / apical constriction / Rho-dependent protein serine/threonine kinase activity / podocyte cell migration / ligand-gated sodium channel activity / regulation of keratinocyte differentiation / positive regulation of phosphatase activity / myoblast migration / positive regulation of connective tissue replacement / membrane to membrane docking / negative regulation of membrane protein ectodomain proteolysis / response to transforming growth factor beta / negative regulation of myosin-light-chain-phosphatase activity / lens morphogenesis in camera-type eye / regulation of cell junction assembly / positive regulation of dephosphorylation / negative regulation of bicellular tight junction assembly / regulation of synapse maturation / bleb / positive regulation of amyloid-beta clearance / melanosome organization / ear development / negative regulation of amyloid precursor protein catabolic process / neuron projection arborization / bleb assembly / embryonic morphogenesis / camera-type eye morphogenesis / leukocyte tethering or rolling / negative regulation of biomineral tissue development / negative regulation of phosphorylation / apical protein localization / actomyosin structure organization / aspartic-type endopeptidase inhibitor activity / regulation of establishment of endothelial barrier / camera-type eye development / RHO GTPases Activate ROCKs / negative regulation of motor neuron apoptotic process / regulation of stress fiber assembly / regulation of cell motility / Sema4D induced cell migration and growth-cone collapse / aortic valve morphogenesis / response to angiotensin / regulation of establishment of cell polarity / motor neuron apoptotic process / RHOBTB1 GTPase cycle / RND3 GTPase cycle / regulation of synaptic vesicle endocytosis / cortical actin cytoskeleton organization / apical junction complex / regulation of neuron differentiation / regulation of focal adhesion assembly / leukocyte cell-cell adhesion / RHOB GTPase cycle / tau-protein kinase activity / leukocyte migration / negative regulation of amyloid-beta formation / EPHA-mediated growth cone collapse / mRNA destabilization / positive regulation of cardiac muscle hypertrophy / RHOC GTPase cycle / Apoptotic cleavage of cellular proteins / positive regulation of focal adhesion assembly / RHOH GTPase cycle / mitotic cytokinesis / Rho protein signal transduction / smooth muscle contraction / RHOA GTPase cycle / bicellular tight junction / epithelial to mesenchymal transition / canonical NF-kappaB signal transduction / regulation of microtubule cytoskeleton organization / positive regulation of autophagy / regulation of cell adhesion / regulation of cell migration / ruffle / EPHB-mediated forward signaling / centriole / blood vessel diameter maintenance / negative regulation of angiogenesis / negative regulation of protein binding / regulation of autophagy / actin filament organization / protein localization to plasma membrane / regulation of actin cytoskeleton organization / adherens junction / brain development / tau protein binding / Schaffer collateral - CA1 synapse / small GTPase binding / beta-catenin binding / VEGFA-VEGFR2 Pathway / cytoplasmic stress granule / neuron projection development / G alpha (12/13) signalling events / actin filament binding / cell migration Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.568 Å | ||||||
Authors | Zalewski, J.K. / VanDemark, A.P. / Heroux, A. | ||||||
Funding support | United States, 1items
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Citation | Journal: J. Biol. Chem. / Year: 2016 Title: Structure of the Shroom-Rho Kinase Complex Reveals a Binding Interface with Monomeric Shroom That Regulates Cell Morphology and Stimulates Kinase Activity. Authors: Zalewski, J.K. / Mo, J.H. / Heber, S. / Heroux, A. / Gardner, R.G. / Hildebrand, J.D. / VanDemark, A.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5f5p.cif.gz | 365.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5f5p.ent.gz | 301.9 KB | Display | PDB format |
PDBx/mmJSON format | 5f5p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f5/5f5p ftp://data.pdbj.org/pub/pdb/validation_reports/f5/5f5p | HTTPS FTP |
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-Related structure data
Related structure data | 5f4yC 3thfS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 24481.703 Da / Num. of mol.: 4 / Fragment: residues 1427-1610 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SHROOM2, APXL / Plasmid: pET151 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) RIPL / References: UniProt: Q13796 #2: Protein | Mass: 10103.093 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ROCK1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) RIPL References: UniProt: Q13464, non-specific serine/threonine protein kinase #3: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.64 Å3/Da / Density % sol: 66.17 % / Description: Thin, square plates |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 20% PEG 3350, 200 mM Magnesium Chloride, 100 mM Tris pH 8.5 PH range: 8.5-8.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Aug 2, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 3.57→50 Å / Num. obs: 21121 / % possible obs: 97.8 % / Redundancy: 5.3 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 24.5 |
Reflection shell | Resolution: 3.57→3.63 Å / Mean I/σ(I) obs: 1.72 / % possible all: 97.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3THF Resolution: 3.568→19.91 Å / SU ML: 0.64 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 41.61 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.568→19.91 Å
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Refine LS restraints |
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LS refinement shell |
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