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Structure paper

TitleA widespread family of molecular chaperones promotes the intracellular stability of type VIIb secretion system-exported toxins.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 122, Page e2503581122-e2503581122, Year 2025
Publish dateAug 27, 2024 (structure data deposition date)
AuthorsGkragkopoulou, P. / Garrett, S.R. / Shah, P.Y. / Grebenc, D.W. / Klein, T.A. / Kim, Y. / Whitney, J.C.
External linksProc. Natl. Acad. Sci. USA / PubMed:40953262
MethodsX-ray diffraction
Resolution1.85 - 3.24 Å
Structure data

PDB-9dcr:
Structure of the TelA-associated type VII secretion system chaperone SIR_0168
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-9dcs:
Structure of a TelD-associated type VII secretion system DUF4176 protein
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-9dct:
Structure of the TelB-associated type VII secretion system chaperone SIR_0178
Method: X-RAY DIFFRACTION / Resolution: 3.24 Å

PDB-9mno:
Structure of the TelA-associated type VII secretion system chaperone LcpA in complex with the chaperone binding site of TelA
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-FMT:
FORMIC ACID

ChemComp-ACY:
ACETIC ACID

ChemComp-CIT:
CITRIC ACID

Source
  • streptococcus intermedius b196 (bacteria)
  • streptococcus intermedius (bacteria)
KeywordsCHAPERONE / Molecular chaperone / type vii secretion system / antibacterial toxins

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