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Yorodumi- PDB-6gbh: Helicobacter pylori adhesin HopQ type II bound to the N-terminal ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6gbh | ||||||
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Title | Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1 | ||||||
Components |
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Keywords | CELL ADHESION / Helicobacter pylori / adhesin / Helicobacter outer membrane protein | ||||||
Function / homology | Function and homology information regulation of endothelial cell differentiation / insulin receptor internalization / regulation of homophilic cell adhesion / negative regulation of cytotoxic T cell degranulation / granulocyte colony-stimulating factor signaling pathway / regulation of sprouting angiogenesis / regulation of epidermal growth factor receptor signaling pathway / regulation of blood vessel remodeling / negative regulation of hepatocyte proliferation / negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target ...regulation of endothelial cell differentiation / insulin receptor internalization / regulation of homophilic cell adhesion / negative regulation of cytotoxic T cell degranulation / granulocyte colony-stimulating factor signaling pathway / regulation of sprouting angiogenesis / regulation of epidermal growth factor receptor signaling pathway / regulation of blood vessel remodeling / negative regulation of hepatocyte proliferation / negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of lipid biosynthetic process / negative regulation of T cell mediated cytotoxicity / bile acid transmembrane transporter activity / regulation of endothelial cell migration / filamin binding / negative regulation of granulocyte differentiation / Fibronectin matrix formation / insulin catabolic process / common myeloid progenitor cell proliferation / negative regulation of interleukin-1 production / negative regulation of fatty acid biosynthetic process / cell-cell adhesion via plasma-membrane adhesion molecules / positive regulation of vasculogenesis / regulation of immune system process / negative regulation of platelet aggregation / bile acid and bile salt transport / negative regulation of vascular permeability / wound healing, spreading of cells / transport vesicle membrane / microvillus membrane / negative regulation of T cell receptor signaling pathway / regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / blood vessel development / homophilic cell adhesion via plasma membrane adhesion molecules / tertiary granule membrane / lateral plasma membrane / specific granule membrane / regulation of cell migration / protein tyrosine kinase binding / basal plasma membrane / regulation of ERK1 and ERK2 cascade / integrin-mediated signaling pathway / regulation of cell growth / Cell surface interactions at the vascular wall / adherens junction / negative regulation of protein kinase activity / kinase binding / cellular response to insulin stimulus / cell-cell junction / cell migration / cell junction / actin binding / protein phosphatase binding / angiogenesis / protein dimerization activity / calmodulin binding / cell adhesion / apical plasma membrane / Neutrophil degranulation / cell surface / signal transduction / protein homodimerization activity / extracellular exosome / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Helicobacter pylori (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.59 Å | ||||||
Authors | Moonens, K. / Kruse, T. / Gerhard, M. / Remaut, H. | ||||||
Citation | Journal: EMBO J. / Year: 2018 Title: Helicobacter pyloriadhesin HopQ disruptstransdimerization in human CEACAMs. Authors: Moonens, K. / Hamway, Y. / Neddermann, M. / Reschke, M. / Tegtmeyer, N. / Kruse, T. / Kammerer, R. / Mejias-Luque, R. / Singer, B.B. / Backert, S. / Gerhard, M. / Remaut, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6gbh.cif.gz | 342 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6gbh.ent.gz | 284.4 KB | Display | PDB format |
PDBx/mmJSON format | 6gbh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gb/6gbh ftp://data.pdbj.org/pub/pdb/validation_reports/gb/6gbh | HTTPS FTP |
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-Related structure data
Related structure data | 6gbgC 2gk2S 5lp2S 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: 12956.362 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CEACAM1, BGP, BGP1 / Production host: Escherichia coli (E. coli) / References: UniProt: P13688 #2: Protein | Mass: 45239.523 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Helicobacter pylori (bacteria) / Gene: hopQ / Production host: Escherichia coli (E. coli) / References: UniProt: Q8GDI6 #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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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: 2.88 Å3/Da / Density % sol: 57.31 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: Condition A4 of the JB Screen Classic HTS II screen (Jena Bioscience) (1 M Ammonium sulfate, 100 mM Tris; pH 8.5) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.98 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 1, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.59→99.05 Å / Num. obs: 42047 / % possible obs: 99.6 % / Redundancy: 9.2 % / Biso Wilson estimate: 67.1 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.123 / Rpim(I) all: 0.043 / Net I/σ(I): 11.7 |
Reflection shell | Resolution: 2.59→2.66 Å / Redundancy: 9 % / Mean I/σ(I) obs: 0.9 / Num. unique obs: 5934 / CC1/2: 0.605 / % possible all: 97.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5LP2, 2GK2 Resolution: 2.59→99.05 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.932 / SU B: 39.384 / SU ML: 0.348 / Cross valid method: THROUGHOUT / ESU R: 0.401 / ESU R Free: 0.295 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 93.221 Å2
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Refinement step | Cycle: 1 / Resolution: 2.59→99.05 Å
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