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Structure paper

TitleArchaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 17070-17080, Year 2018
Publish dateJan 30, 2018 (structure data deposition date)
AuthorsPakharukova, N. / McKenna, S. / Tuittila, M. / Paavilainen, S. / Malmi, H. / Xu, Y. / Parilova, O. / Matthews, S. / Zavialov, A.V.
External linksJ. Biol. Chem. / PubMed:30228191
MethodsX-ray diffraction
Resolution1.47 - 2.85 Å
Structure data

PDB-6fm5:
Crystal structure of self-complemented CsuA/B major subunit from archaic chaperone-usher Csu pili of Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 1.47 Å

PDB-6fq0:
Crystal structure of the CsuC-CsuA/B chaperone-subunit preassembly complex of the archaic chaperone-usher Csu pili of Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6fqa:
Crystal structure of the CsuC-CsuA/B chaperone-subunit preassembly complex of the archaic chaperone-usher Csu pili of Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • acinetobacter baumannii (bacteria)
KeywordsCELL ADHESION / Ig-like fold / beta sandwich / donor-strand complementation

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