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Structure paper

TitleThe F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 65, Page 411-420, Year 2009
Publish dateNov 5, 2008 (structure data deposition date)
AuthorsVan Molle, I. / Moonens, K. / Buts, L. / Garcia-Pino, A. / Panjikar, S. / Wyns, L. / De Greve, H. / Bouckaert, J.
External linksActa Crystallogr. ,Sect. D / PubMed:19390146
MethodsX-ray diffraction
Resolution2.29 - 2.801 Å
Structure data

PDB-3f65:
The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

PDB-3f6i:
Structure of the SeMet labeled F4 fibrial chaperone FaeE
Method: X-RAY DIFFRACTION / Resolution: 2.788 Å

PDB-3f6l:
Structure of the F4 fimbrial chaperone FaeE
Method: X-RAY DIFFRACTION / Resolution: 2.801 Å

Chemicals

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsCHAPERONE / immunoglobulin-like fold / Cell projection / Fimbrium / Immunoglobulin domain / Periplasm / Plasmid

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