Home > Publications database > The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces > print

001     94240
005     20250731122622.0
024 7 _ |a pmid:19390146
|2 pmid
024 7 _ |a 10.1107/S0907444909005174
|2 doi
024 7 _ |a 0907-4449
|2 ISSN
024 7 _ |a 1399-0047
|2 ISSN
024 7 _ |a WOS:000265267000002
|2 WOS
024 7 _ |a openalex:W2005808201
|2 openalex
037 _ _ |a PHPPUBDB-12662
041 _ _ |a eng
082 _ _ |a 570
100 1 _ |a Van Molle, I.
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces
260 _ _ |a Copenhagen
|c 2009
|b Munksgaard
300 _ _ |a 411-420
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1542743454_10484
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
440 _ 0 |a Acta Crystallogr. D, Biol. Crystall.
|0 PERI:(DE-600)2020492-9
|v 65
|x 0907-4449
500 _ _ |a © International Union of Crystallography; Post referee fulltext in progress
|3 Converted on 2013-05-30 14:57
500 _ _ |3 Converted on 2013-06-21 19:21
520 _ _ |a Many Gram-negative bacteria use the chaperone-usher pathway to express adhesive surface structures, such as fimbriae, in order to mediate attachment to host cells. Periplasmic chaperones are required to shuttle fimbrial subunits or pilins through the periplasmic space in an assembly-competent form. The chaperones cap the hydrophobic surface of the pilins through a donor-strand complementation mechanism. FaeE is the periplasmic chaperone required for the assembly of the F4 fimbriae of enterotoxigenic Escherichia coli. The FaeE crystal structure shows a dimer formed by interaction between the pilin-binding interfaces of the two monomers. Dimerization and tetramerization have been observed previously in crystal structures of fimbrial chaperones and have been suggested to serve as a self-capping mechanism that protects the pilin-interactive surfaces in solution in the absence of the pilins. However, thermodynamic and biochemical data show that FaeE occurs as a stable monomer in solution. Other lines of evidence indicate that self-capping of the pilin-interactive interfaces is not a mechanism that is conservedly applied by all periplasmic chaperones, but is rather a case-specific solution to cap aggregation-prone surfaces.
536 _ _ |0 G:(DE-H253)POF1-No-Ref-20130405
|f POF I
|x 0
|c POF1-550
|a FS Beamline without reference (POF1-550)
588 _ _ |a Dataset connected to Pubmed
650 _ 7 |a Adhesins, Escherichia coli
|0 0
|2 NLM Chemicals
650 _ 7 |a Cross-Linking Reagents
|0 0
|2 NLM Chemicals
650 _ 7 |a Escherichia coli Proteins
|0 0
|2 NLM Chemicals
650 _ 7 |a FaeG protein, E coli
|0 0
|2 NLM Chemicals
650 _ 7 |a Molecular Chaperones
|0 0
|2 NLM Chemicals
650 _ 7 |a Recombinant Fusion Proteins
|0 0
|2 NLM Chemicals
650 _ 7 |a Glutaral
|0 111-30-8
|2 NLM Chemicals
650 _ 7 |a faeE protein, E coli
|0 138341-60-3
|2 NLM Chemicals
650 _ 7 |a Fimbriae Proteins
|0 147680-16-8
|2 NLM Chemicals
650 _ 2 |a Adhesins, Escherichia coli: chemistry
|2 MeSH
650 _ 2 |a Calorimetry, Differential Scanning
|2 MeSH
650 _ 2 |a Cross-Linking Reagents: pharmacology
|2 MeSH
650 _ 2 |a Crystallography, X-Ray
|2 MeSH
650 _ 2 |a Dimerization
|2 MeSH
650 _ 2 |a Escherichia coli: chemistry
|2 MeSH
650 _ 2 |a Escherichia coli: genetics
|2 MeSH
650 _ 2 |a Escherichia coli Proteins: chemistry
|2 MeSH
650 _ 2 |a Escherichia coli Proteins: genetics
|2 MeSH
650 _ 2 |a Escherichia coli Proteins: isolation & purification
|2 MeSH
650 _ 2 |a Escherichia coli Proteins: metabolism
|2 MeSH
650 _ 2 |a Fimbriae Proteins: metabolism
|2 MeSH
650 _ 2 |a Glutaral: pharmacology
|2 MeSH
650 _ 2 |a Models, Molecular
|2 MeSH
650 _ 2 |a Molecular Chaperones: chemistry
|2 MeSH
650 _ 2 |a Molecular Chaperones: genetics
|2 MeSH
650 _ 2 |a Molecular Chaperones: isolation & purification
|2 MeSH
650 _ 2 |a Molecular Chaperones: metabolism
|2 MeSH
650 _ 2 |a Nephelometry and Turbidimetry
|2 MeSH
650 _ 2 |a Protein Conformation
|2 MeSH
650 _ 2 |a Protein Denaturation
|2 MeSH
650 _ 2 |a Protein Interaction Mapping
|2 MeSH
650 _ 2 |a Recombinant Fusion Proteins: chemistry
|2 MeSH
650 _ 2 |a Recombinant Fusion Proteins: isolation & purification
|2 MeSH
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|f Unknown DESY Beamline
700 1 _ |a Moonens, K.
700 1 _ |a Buts, L.
700 1 _ |a Garcia-Pino, A.
700 1 _ |a Panjikar, S.
700 1 _ |a Wyns, L.
700 1 _ |a De Greve, H.
700 1 _ |a Bouckaert, J.
773 _ _ |a 10.1107/S0907444909005174
|g Vol. 65, p. 411-420
|0 PERI:(DE-600)2020492-9
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|p 411-420
|t Acta crystallographica / D
|v 65
|y 2009
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910 1 _ |a Externes Institut
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913 1 _ |0 G:(DE-HGF)POF1-550
|v Großgeräte für die Forschung mit Photonen, Neutronen, Ionen
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|2 G:(DE-HGF)POF1-500
|b Struktur der Materie
|l Großgeräte für die Forschung mit Photonen, Neutronen, Ionen
914 1 _ |y 2009
915 _ _ |a DBCoverage
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915 _ _ |a No Authors Fulltext
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920 _ _ |k 001
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920 _ 1 |i Experiments with synchrotron radiation
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980 _ _ |a journal
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980 _ _ |a UNRESTRICTED
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