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- PDB-4cc4: Complex of InlC of Listeria monocytogenes and human Tuba C-termin... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4cc4 | |||||||||
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Title | Complex of InlC of Listeria monocytogenes and human Tuba C-terminal SH3 domain | |||||||||
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![]() | CELL INVASION / BACTERIAL INFECTION / PATHOGENESIS / LISTERIAL CELL-CELL SPREAD / VIRULENCE FACTOR / PROTEIN-PROTEIN INTERACTIONS / LEUCINE-RICH REPEAT / SRC HOMOLOGY 3 DOMAIN / DISRUPTION OF CORTICAL TENSION / CELL MEMBRANE PROTRUSIONS | |||||||||
Function / homology | ![]() Golgi stack / regulation of small GTPase mediated signal transduction / CDC42 GTPase cycle / cilium assembly / guanyl-nucleotide exchange factor activity / cell-cell junction / presynapse / regulation of cell shape / host cell cytoplasm / cytoskeleton ...Golgi stack / regulation of small GTPase mediated signal transduction / CDC42 GTPase cycle / cilium assembly / guanyl-nucleotide exchange factor activity / cell-cell junction / presynapse / regulation of cell shape / host cell cytoplasm / cytoskeleton / intracellular signal transduction / synapse / Golgi apparatus / extracellular region / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Polle, L. / Rigano, L. / Julian, R. / Ireton, K. / Schubert, W.-D. | |||||||||
![]() | ![]() Title: Structural Details of Human Tuba Recruitment by Inlc of Listeria Monocytogenes Elucidate Bacterial Cell-Cell Spreading. Authors: Polle, L. / Rigano, L.A. / Julian, R. / Ireton, K. / Schubert, W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 424.2 KB | Display | ![]() |
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PDB format | ![]() | 349.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 697.5 KB | Display | ![]() |
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Full document | ![]() | 712.2 KB | Display | |
Data in XML | ![]() | 41.2 KB | Display | |
Data in CIF | ![]() | 57.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4cc2C ![]() 4cc3C ![]() 4cc7C ![]() 1xeuS ![]() 1zuuS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
-Protein , 3 types, 6 molecules AEBDFC
#1: Protein | Mass: 29718.535 Da / Num. of mol.: 2 / Fragment: INTERNALIN DOMAIN, RESIDUES 35-297 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() #2: Protein | Mass: 7783.694 Da / Num. of mol.: 3 / Fragment: C-TERMINAL SH3 DOMAIN OF TUBA, RESIDUES 1513-1577 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Protein | | Mass: 29702.535 Da / Num. of mol.: 1 / Fragment: INTERNALIN DOMAIN, RESIDUES 35-297 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() |
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-Non-polymers , 6 types, 296 molecules ![](data/chem/img/GOL.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/PE4.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/PE4.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-GOL / #5: Chemical | ChemComp-CL / #6: Chemical | ChemComp-PE4 / | #7: Chemical | #8: Chemical | #9: Water | ChemComp-HOH / | |
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-Details
Sequence details | 3 N-TERMINAL AMINO ACIDS DERIVE FROM FUSION PROTEIN CLEAVAGE SITE N-TERMINAL TWO RESIDUES GP DERIVE ...3 N-TERMINAL AMINO ACIDS DERIVE FROM FUSION PROTEIN CLEAVAGE SITE N-TERMINAL TWO RESIDUES GP DERIVE FROM FUSION PROTEIN CLEAVAGE |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52 % / Description: NONE |
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Crystal grow | pH: 7.5 / Details: 0.8 M NA2HPO4, 0.8 M K2HPO4, 0.1 M HEPES PH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU SATURN 944 / Detector: CCD / Date: May 3, 2011 / Details: OSMIC VARIMAX |
Radiation | Monochromator: OSMIC VARIMAX / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→15 Å / Num. obs: 36275 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 5.5 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 21.4 |
Reflection shell | Resolution: 2.6→2.64 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.66 / Mean I/σ(I) obs: 3 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 1XEU, 1ZUU Resolution: 2.6→14.97 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.912 / SU B: 23.93 / SU ML: 0.258 / Cross valid method: THROUGHOUT / ESU R: 1.892 / ESU R Free: 0.344 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.N U VALUES WITH TLS ADDED
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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: 50.137 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→14.97 Å
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Refine LS restraints |
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