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TitleChaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 111, Page 543-551, Year 2002
Publish dateOct 14, 2002 (structure data deposition date)
AuthorsSauer, F.G. / Pinkner, J.S. / Waksman, G. / Hultgren, S.J.
External linksCell(Cambridge,Mass. ) / PubMed:12437927
MethodsX-ray diffraction
Resolution1.87 - 2.3 Å
Structure data

PDB-1n0l:
Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1n12:
Crystal structure of the PapE (N-terminal-deleted) pilus subunit bound to a peptide corresponding to the N-terminal extension of the PapK pilus subunit (residues 1-11) from uropathogenic E. coli
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsCHAPERONE / Immunoglobulin-like fold / donor strand complemenation / donor strand exchange / chaperone priming / pilus fiber assembly / donor strand complementation / organelle biogenesis

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