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Yorodumi- PDB-2lnh: Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lnh | ||||||
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Title | Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to hijack host F-actin assembly | ||||||
Components |
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Keywords | Signaling Protein/Protein Binding / Protein complex / Signaling Protein-Protein Binding complex | ||||||
Function / homology | Function and homology information negative regulation of membrane tubulation / spindle localization / positive regulation of clathrin-dependent endocytosis / negative regulation of lymphocyte migration / NOSTRIN mediated eNOS trafficking / GTPase regulator activity / actin cap / plasma membrane organization / vesicle organization / actin crosslink formation ...negative regulation of membrane tubulation / spindle localization / positive regulation of clathrin-dependent endocytosis / negative regulation of lymphocyte migration / NOSTRIN mediated eNOS trafficking / GTPase regulator activity / actin cap / plasma membrane organization / vesicle organization / actin crosslink formation / vesicle transport along actin filament / cadherin binding involved in cell-cell adhesion / vesicle budding from membrane / actin polymerization or depolymerization / protein-containing complex localization / dendritic spine morphogenesis / RHOF GTPase cycle / proline-rich region binding / Nephrin family interactions / DCC mediated attractive signaling / positive regulation of filopodium assembly / regulation of postsynapse organization / RHOV GTPase cycle / positive regulation of actin filament polymerization / RHOJ GTPase cycle / RHOQ GTPase cycle / actin filament bundle assembly / CDC42 GTPase cycle / RAC2 GTPase cycle / RHO GTPases Activate WASPs and WAVEs / RAC3 GTPase cycle / EPHB-mediated forward signaling / RAC1 GTPase cycle / actin filament polymerization / regulation of actin cytoskeleton organization / adherens junction / FCGR3A-mediated phagocytosis / response to bacterium / Regulation of actin dynamics for phagocytic cup formation / regulation of protein localization / endocytic vesicle membrane / Clathrin-mediated endocytosis / actin cytoskeleton / lamellipodium / actin binding / cytoplasmic vesicle / microtubule binding / protein-containing complex assembly / host cell cytoplasm / cytoskeleton / cell division / glutamatergic synapse / endoplasmic reticulum membrane / positive regulation of transcription by RNA polymerase II / extracellular exosome / extracellular region / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Escherichia coli O157:H7 (bacteria) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, molecular dynamics | ||||||
Model details | fewest violations, model 1 | ||||||
Authors | Aitio, O. / Hellman, M. / Skehan, B. / Kesti, T. / Leong, J.M. / Saksela, K. / Permi, P. | ||||||
Citation | Journal: Structure / Year: 2012 Title: Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Authors: Aitio, O. / Hellman, M. / Skehan, B. / Kesti, T. / Leong, J.M. / Saksela, K. / Permi, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lnh.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2lnh.ent.gz | 916.5 KB | Display | PDB format |
PDBx/mmJSON format | 2lnh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lnh_validation.pdf.gz | 446 KB | Display | wwPDB validaton report |
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Full document | 2lnh_full_validation.pdf.gz | 814.2 KB | Display | |
Data in XML | 2lnh_validation.xml.gz | 69.1 KB | Display | |
Data in CIF | 2lnh_validation.cif.gz | 90.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ln/2lnh ftp://data.pdbj.org/pub/pdb/validation_reports/ln/2lnh | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7262.023 Da / Num. of mol.: 1 / Fragment: UNP residues 207-270 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: WASL / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O00401 |
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#2: Protein | Mass: 7559.607 Da / Num. of mol.: 1 / Fragment: SH3 domain residues 339-402 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BAIAP2L1, IRTKS / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9UHR4 |
#3: Protein/peptide | Mass: 5301.970 Da / Num. of mol.: 1 / Fragment: UNP residues 221-267 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli O157:H7 (bacteria) / Strain: O157:H7 / Gene: espF(U), tccP / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0DJ89 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 50 / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20 |