[English] 日本語
![](img/lk-miru.gif)
- SASDAA9: EcPaaA2-EcParE2His construct (Plasmid stabilization protein ParE,... -
+
Open data
-
Basic information
Entry | Database: SASBDB / ID: SASDAA9 |
---|---|
![]() | EcPaaA2-EcParE2His construct
|
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 / : ![]() |
Biological species | ![]() ![]() |
![]() | ![]() 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. |
![]() |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-Models
Model #354 | ![]() Type: mix / Radius of dummy atoms: 1.90 A / Comment: NMA refinement / Chi-square value: 1.170 ![]() |
---|---|
Model #357 | ![]() Type: dummy / Radius of dummy atoms: 3.75 A / Symmetry: P1 / Chi-square value: 0.691 ![]() |
-
Sample
![]() | Name: EcPaaA2-EcParE2His construct / Specimen concentration: 0.50-3.50 / Entity id: 213 / 214 |
---|---|
Buffer | Name: 50 mM Tris-HCl 500 mM NaCl / Concentration: 50.00 mM / pH: 7.5 / Composition: 500 mM NaCl |
Entity #213 | Name: EcParE2His / Type: protein / Description: Plasmid stabilization protein ParE / Formula weight: 11.726 / Num. of mol.: 16 / Source: Escherichia coli / References: UniProt: A0A0D7C2L1 Sequence: MLPVLWLESA DTDLDDITSY IARFDIDAAE RLWQRLRGCV LPLSEHPYLY PPSDRVPGLR EIVAHPNYII LYRVTTSSVE VVNVIHARRQ FPLEHHHHHH |
Entity #214 | Name: EcPaaA2 / Type: protein / Description: Uncharacterized protein (Antitoxin) / Formula weight: 8.458 / Num. of mol.: 16 / Source: Escherichia coli / References: UniProt: A0A0F6F6Q9 Sequence: MDYKDDDDKN RALSPMVSEF ETIEQENSYN EWLRAKVATS LADPRPAIPH DEVERRMAER FAKMRKERSK Q |
-Experimental information
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France ![]() | |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Detector | Name: Pilatus 1M | |||||||||||||||||||||
Scan |
| |||||||||||||||||||||
Distance distribution function P(R) |
| |||||||||||||||||||||
Result | Comments: Use of SAXS to validate the oligomer state of the obtained crystal structure and to model missing afinity tags
|