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Yorodumi- SASDAB9: EcPaaA2-HisEcParE2 construct (Plasmid stabilization protein ParE,... -
+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDAB9 |
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Sample | EcPaaA2-HisEcParE2 construct
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Function / homology | : / ParE toxin of type II toxin-antitoxin system, parDE / Toxin-antitoxin system, RelE/ParE toxin family / Toxin-antitoxin system, RelE/ParE toxin domain superfamily / Plasmid stabilization protein ParE / : Function and homology information |
Biological species | Escherichia coli (E. coli) |
Citation | Journal: J Mol Biol / Year: 2016 Title: A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. Authors: Yann G-J Sterckx / Thomas Jové / Alexander V Shkumatov / Abel Garcia-Pino / Lieselotte Geerts / Maia De Kerpel / Jurij Lah / Henri De Greve / Laurence Van Melderen / Remy Loris / Abstract: Many bacterial pathogens modulate their metabolic activity, virulence and pathogenicity through so-called "toxin-antitoxin" (TA) modules. The genome of the human pathogen Escherichia coli O157 ...Many bacterial pathogens modulate their metabolic activity, virulence and pathogenicity through so-called "toxin-antitoxin" (TA) modules. The genome of the human pathogen Escherichia coli O157 contains two three-component TA modules related to the known parDE module. Here, we show that the toxin EcParE2 maps in a branch of the RelE/ParE toxin superfamily that is distinct from the branches that contain verified gyrase and ribosome inhibitors. The structure of EcParE2 closely resembles that of Caulobacter crescentus ParE but shows a distinct pattern of conserved surface residues, in agreement with its apparent inability to interact with GyrA. The antitoxin EcPaaA2 is characterized by two α-helices (H1 and H2) that serve as molecular recognition elements to wrap itself around EcParE2. Both EcPaaA2 H1 and H2 are required to sustain a high-affinity interaction with EcParE2 and for the inhibition of EcParE2-mediated killing in vivo. Furthermore, evidence demonstrates that EcPaaA2 H2, but not H1, determines specificity for EcParE2. The initially formed EcPaaA2-EcParE2 heterodimer then assembles into a hetero-hexadecamer, which is stable in solution and is formed in a highly cooperative manner. Together these findings provide novel data on quaternary structure, TA interactions and activity of a hitherto poorly characterized family of TA modules. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Models
Model #355 | Type: mix / Radius of dummy atoms: 1.90 A / Comment: NMA refinement / Chi-square value: 3.439 Search similar-shape structures of this assembly by Omokage search (details) |
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Model #356 | Type: dummy / Radius of dummy atoms: 3.50 A / Chi-square value: 0.637 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: EcPaaA2-HisEcParE2 construct / Specimen concentration: 1.00-10.00 / Entity id: 215 / 216 |
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Buffer | Name: 50 mM Tris-HCl 500 mM NaCl / Concentration: 50.00 mM / pH: 7.5 / Composition: 500 mM NaCl |
Entity #215 | Name: EcParE2 / Type: protein / Description: Plasmid stabilization protein ParE / Formula weight: 12.693 / Num. of mol.: 8 / Source: Escherichia coli / References: UniProt: A0A0D7C2L1 Sequence: MGSSHHHHHH SSGLVPRGSH LPVLWLESAD TDLDDITSYI ARFDIDAAER LWQRLRGCVL PLSEHPYLYP PSDRVPGLRE IVAHPNYIIL YRVTTSSVEV VNVIHARRQF P |
Entity #216 | Name: EcPaaA2 / Type: protein / Description: Uncharacterized protein (Antitoxin) / Formula weight: 8.458 / Num. of mol.: 8 / Source: Escherichia coli / References: UniProt: A0A0F6F6Q9 Sequence: MDYKDDDDKN RALSPMVSEF ETIEQENSYN EWLRAKVATS LADPRPAIPH DEVERRMAER FAKMRKERSK Q |
-Experimental information
Beam | Instrument name: SOLEIL SWING / City: Saint-Aubin / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 1.82 mm | |||||||||||||||||||||
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Detector | Name: AVIEX / Type: CCD | |||||||||||||||||||||
Scan | Title: parDE-like toxin-antitoxin module / Measurement date: Feb 5, 2012 / Cell temperature: 10 °C / Exposure time: 0.75 sec. / Number of frames: 750 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 386 /
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Result | D max: 15.28 / Type of curve: merged Comments: Use of SAXS to validate the oligomer state of the obtained crystal structure and to model missing afinity tags
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