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000094240 1001_ $$aVan Molle, I.
000094240 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000094240 245__ $$aThe F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces
000094240 260__ $$aCopenhagen$$bMunksgaard$$c2009
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000094240 440_0 $$0PERI:(DE-600)2020492-9$$aActa Crystallogr. D, Biol. Crystall.$$v65$$x0907-4449
000094240 500__ $$3Converted on 2013-05-30 14:57$$a© International Union of Crystallography; Post referee fulltext in progress 
000094240 500__ $$3Converted on 2013-06-21 19:21
000094240 520__ $$aMany Gram-negative bacteria use the chaperone-usher pathway to express adhesive surface structures, such as fimbriae, in order to mediate attachment to host cells. Periplasmic chaperones are required to shuttle fimbrial subunits or pilins through the periplasmic space in an assembly-competent form. The chaperones cap the hydrophobic surface of the pilins through a donor-strand complementation mechanism. FaeE is the periplasmic chaperone required for the assembly of the F4 fimbriae of enterotoxigenic Escherichia coli. The FaeE crystal structure shows a dimer formed by interaction between the pilin-binding interfaces of the two monomers. Dimerization and tetramerization have been observed previously in crystal structures of fimbrial chaperones and have been suggested to serve as a self-capping mechanism that protects the pilin-interactive surfaces in solution in the absence of the pilins. However, thermodynamic and biochemical data show that FaeE occurs as a stable monomer in solution. Other lines of evidence indicate that self-capping of the pilin-interactive interfaces is not a mechanism that is conservedly applied by all periplasmic chaperones, but is rather a case-specific solution to cap aggregation-prone surfaces.
000094240 536__ $$0G:(DE-H253)POF1-No-Ref-20130405$$aFS Beamline without reference (POF1-550)$$cPOF1-550$$fPOF I$$x0
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000094240 650_7 $$00$$2NLM Chemicals$$aAdhesins, Escherichia coli
000094240 650_7 $$00$$2NLM Chemicals$$aCross-Linking Reagents
000094240 650_7 $$00$$2NLM Chemicals$$aEscherichia coli Proteins
000094240 650_7 $$00$$2NLM Chemicals$$aFaeG protein, E coli
000094240 650_7 $$00$$2NLM Chemicals$$aMolecular Chaperones
000094240 650_7 $$00$$2NLM Chemicals$$aRecombinant Fusion Proteins
000094240 650_7 $$0111-30-8$$2NLM Chemicals$$aGlutaral
000094240 650_7 $$0138341-60-3$$2NLM Chemicals$$afaeE protein, E coli
000094240 650_7 $$0147680-16-8$$2NLM Chemicals$$aFimbriae Proteins
000094240 650_2 $$2MeSH$$aAdhesins, Escherichia coli: chemistry
000094240 650_2 $$2MeSH$$aCalorimetry, Differential Scanning
000094240 650_2 $$2MeSH$$aCross-Linking Reagents: pharmacology
000094240 650_2 $$2MeSH$$aCrystallography, X-Ray
000094240 650_2 $$2MeSH$$aDimerization
000094240 650_2 $$2MeSH$$aEscherichia coli: chemistry
000094240 650_2 $$2MeSH$$aEscherichia coli: genetics
000094240 650_2 $$2MeSH$$aEscherichia coli Proteins: chemistry
000094240 650_2 $$2MeSH$$aEscherichia coli Proteins: genetics
000094240 650_2 $$2MeSH$$aEscherichia coli Proteins: isolation & purification
000094240 650_2 $$2MeSH$$aEscherichia coli Proteins: metabolism
000094240 650_2 $$2MeSH$$aFimbriae Proteins: metabolism
000094240 650_2 $$2MeSH$$aGlutaral: pharmacology
000094240 650_2 $$2MeSH$$aModels, Molecular
000094240 650_2 $$2MeSH$$aMolecular Chaperones: chemistry
000094240 650_2 $$2MeSH$$aMolecular Chaperones: genetics
000094240 650_2 $$2MeSH$$aMolecular Chaperones: isolation & purification
000094240 650_2 $$2MeSH$$aMolecular Chaperones: metabolism
000094240 650_2 $$2MeSH$$aNephelometry and Turbidimetry
000094240 650_2 $$2MeSH$$aProtein Conformation
000094240 650_2 $$2MeSH$$aProtein Denaturation
000094240 650_2 $$2MeSH$$aProtein Interaction Mapping
000094240 650_2 $$2MeSH$$aRecombinant Fusion Proteins: chemistry
000094240 650_2 $$2MeSH$$aRecombinant Fusion Proteins: isolation & purification
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000094240 7001_ $$aMoonens, K.
000094240 7001_ $$aButs, L.
000094240 7001_ $$aGarcia-Pino, A.
000094240 7001_ $$aPanjikar, S.
000094240 7001_ $$aWyns, L.
000094240 7001_ $$aDe Greve, H.
000094240 7001_ $$aBouckaert, J.
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