Literature DB >> 16511060

Crystallization of the FaeE chaperone of Escherichia coli F4 fimbriae.

Inge Van Molle1, Lieven Buts, Fanny Coppens, Liu Qiang, Lode Wyns, Remy Loris, Julie Bouckaert, Henri De Greve.   

Abstract

F4 (formerly K88) fimbriae from enterotoxigenic Escherichia coli are assembled via the FaeE/FaeD chaperone/usher pathway. The chaperone FaeE crystallizes in three crystal forms, all belonging to space group C2. Crystals of form 1 diffract to 2.3 A and have unit-cell parameters a = 195.7, b = 78.5, c = 184.6 A, beta = 102.2 degrees. X-ray data for crystal form 2 were collected to 2.7 A using an SeMet variant of FaeE. The crystals have unit-cell parameters a = 136.4, b = 75.7, c = 69.4 A, beta = 92.8 degrees. Crystals of form 3 were formed in a solution containing the FaeE-FaeG complex and diffract to 2.8 A. Unit-cell parameters are a = 109.7, b = 78.6, c = 87.8 A, beta = 96.4 degrees.

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Year:  2005        PMID: 16511060      PMCID: PMC1952412          DOI: 10.1107/S1744309105008432

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  21 in total

1.  Structural basis of chaperone function and pilus biogenesis.

Authors:  F G Sauer; K Fütterer; J S Pinkner; K W Dodson; S J Hultgren; G Waksman
Journal:  Science       Date:  1999-08-13       Impact factor: 47.728

2.  X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli.

Authors:  D Choudhury; A Thompson; V Stojanoff; S Langermann; J Pinkner; S J Hultgren; S D Knight
Journal:  Science       Date:  1999-08-13       Impact factor: 47.728

3.  Structural basis of chaperone self-capping in P pilus biogenesis.

Authors:  D L Hung; J S Pinkner; S D Knight; S J Hultgren
Journal:  Proc Natl Acad Sci U S A       Date:  1999-07-06       Impact factor: 11.205

4.  PapD-like chaperones provide the missing information for folding of pilin proteins.

Authors:  M M Barnhart; J S Pinkner; G E Soto; F G Sauer; S Langermann; G Waksman; C Frieden; S J Hultgren
Journal:  Proc Natl Acad Sci U S A       Date:  2000-07-05       Impact factor: 11.205

Review 5.  The chaperone/usher pathway: a major terminal branch of the general secretory pathway.

Authors:  D G Thanassi; E T Saulino; S J Hultgren
Journal:  Curr Opin Microbiol       Date:  1998-04       Impact factor: 7.934

Review 6.  Chaperone-assisted pilus assembly and bacterial attachment.

Authors:  F G Sauer; M Barnhart; D Choudhury; S D Knight; G Waksman; S J Hultgren
Journal:  Curr Opin Struct Biol       Date:  2000-10       Impact factor: 6.809

7.  Structure of the S pilus periplasmic chaperone SfaE at 2.2 A resolution.

Authors:  Stefan D Knight; Devapriya Choudhury; Scott Hultgren; Jerome Pinkner; Vivian Stojanoff; Andrew Thompson
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2002-05-29

8.  The CCP4 suite: programs for protein crystallography.

Authors: 
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1994-09-01

9.  Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.

Authors:  D J Leahy; W A Hendrickson; I Aukhil; H P Erickson
Journal:  Science       Date:  1992-11-06       Impact factor: 47.728

10.  Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.

Authors:  A Holmgren; M J Kuehn; C I Brändén; S J Hultgren
Journal:  EMBO J       Date:  1992-04       Impact factor: 11.598

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  1 in total

1.  Structure of CfaA suggests a new family of chaperones essential for assembly of class 5 fimbriae.

Authors:  Rui Bao; April Fordyce; Yu-Xing Chen; Annette McVeigh; Stephen J Savarino; Di Xia
Journal:  PLoS Pathog       Date:  2014-08-14       Impact factor: 6.823

  1 in total

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