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TitleStructural and functional characterization of the IpaD pi-helix reveals critical roles in DOC interaction, T3SS apparatus maturation, and Shigella virulence.
Journal, issue, pagesJ. Biol. Chem., Vol. 300, Page 107613-107613, Year 2024
Publish dateNov 30, 2023 (structure data deposition date)
AuthorsBarker, S.A. / Bernard, A.R. / Morales, Y. / Johnson, S.J. / Dickenson, N.E.
External linksJ. Biol. Chem. / PubMed:39079629
MethodsX-ray diffraction
Resolution1.96 - 3 Å
Structure data

PDB-8v5c:
IpaD (122-321) Bound to Deoxycholate
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

PDB-8v5e:
IpaD (122-321) Pi-helix Mutant (delta Q148) Bound to Deoxycholate
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-8v7q:
IpaD (122-321) Pi-helix Mutant (delta Q148) Apo Structure
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-8v7s:
IpaD (122-321) Apo Structure
Method: X-RAY DIFFRACTION / Resolution: 2.708 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-DXC:
(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID / detergent*YM

ChemComp-HOH:
WATER

Source
  • shigella flexneri (bacteria)
KeywordsCELL INVASION / T3SS / Shigella / Pi-helix / Deoxycholate / Type Three Secretion System / T3SA / Pi helix / Deoxycholate bound

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