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TitleA unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex.
Journal, issue, pagesJ Mol Biol, Vol. 428, Issue 8, Page 1589-1603, Year 2016
Publish dateApr 24, 2016
AuthorsYann 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 /
PubMed AbstractMany 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.
External linksJ Mol Biol / PubMed:26996937
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.671 - 3.82 Å
Structure data

SASDAA9:
EcPaaA2-EcParE2His construct (Plasmid stabilization protein ParE, EcParE2His + Uncharacterized protein (Antitoxin), EcPaaA2)
Method: SAXS/SANS

SASDAB9:
EcPaaA2-HisEcParE2 construct (Plasmid stabilization protein ParE, EcParE2 + Uncharacterized protein (Antitoxin), EcPaaA2)
Method: SAXS/SANS

SASDC84:
parDE-like toxin-antitoxin module, EcPaaA2_13-63-HisEcParE2 construct
Method: SAXS/SANS

PDB-5cw7:
Crystal structure of the PaaA2-ParE2 antitoxin-toxin complex
Method: X-RAY DIFFRACTION / Resolution: 2.827 Å

PDB-5cze:
Crystal structure of the PaaA2-ParE2 antitoxin-toxin complex
Method: X-RAY DIFFRACTION / Resolution: 3.82 Å

PDB-5czf:
Crystal structure of the PaaA2-ParE2 antitoxin-toxin complex
Method: X-RAY DIFFRACTION / Resolution: 2.671 Å

Chemicals

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

ChemComp-SO4:
SULFATE ION / Sulfate

Source
  • Escherichia coli (E. coli)
  • escherichia coli o157:h7 str. ss52 (bacteria)
  • escherichia coli o157 (bacteria)
KeywordsTOXIN / toxin-antitoxin

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