The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

ECs0154  -  ferrichrome outer membrane transporter

Escherichia coli O157:H7 str. Sakai

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ECs0154


High impact information on ECs0154

  • Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes [1].
  • Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide [6].
  • These data suggest that binding of T5 to loop 322-355 of FhuA, which constitutes the T5 binding site, unmasks an inner channel in FhuA [2].
  • The transport-active conformation of FhuA is mediated by a TonB-induced conformational change in response to the energized cytoplasmic membrane [7].
  • When T5 phage binds to its membrane protein receptor, FhuA, its double stranded DNA (120,000 bp) is progressively released base pair after base pair in the surrounding medium [8].

Chemical compound and disease context of ECs0154


Biological context of ECs0154


Anatomical context of ECs0154

  • During siderophore transport into the periplasm, the FhuA cork domain has been proposed to undergo conformational changes that allow transport through the barrel lumen; alternatively, the cork may be completely displaced from the barrel [16].

Associations of ECs0154 with chemical compounds

  • These results indicate that, in vivo, the binding of ferricrocin to FhuA enhances complex formation between the receptor and TonB [17].
  • We exchanged and deleted the N termini of two such siderophore receptors, FepA and FhuA, which recognize and transport ferric enterobactin and ferrichrome, respectively [18].
  • Conversely, a monoclonal antibody that binds near the N terminus of FhuA reduced the retention of TonB by histidine-tagged FhuA [17].
  • Results from trypsin digestion were interpreted as a conformational change in FhuA which had occurred upon ferrichrome binding, thereby preventing access of trypsin to lysine 67 [19].
  • Analyses of these sequences using the Receptor Ligand Contacts (RELIC) suite of programs revealed clusters of multiply aligned peptides that mapped to FhuA [20].

Analytical, diagnostic and therapeutic context of ECs0154

  • Using cryoelectron microscopy, we have visualized the structures formed after T5 phage DNA is released into neutral unilamellar proteoliposomes reconstituted with the receptor FhuA [8].
  • Subsequent SDS-PAGE analysis revealed two distinct species: FhuA containing a disulfide bond and FhuA with free sulfhydryl groups [16].
  • Direct interaction of pb5 with FhuA was demonstrated by isolating a pb5/FhuA complex using size-exclusion chromatography [21].
  • SDS-PAGE and differential scanning calorimetry experiments highlighted the great stability of the complex: (i) it was not dissociated by 2% SDS even when the temperature was raised to 70 degrees C; (ii) thermal denaturation of the complex occurred at 85 degrees C, while pb5 and FhuA were denatured at 45 degrees C and 74 degrees C, respectively [21].
  • Isothermal titration calorimetry measurements demonstrate that TonB-CTD interacts with the FhuA-derived peptide with a K(D)=36(+/-7) microM [22].


  1. Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Locher, K.P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J.P., Moras, D. Cell (1998) [Pubmed]
  2. FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5. Bonhivers, M., Ghazi, A., Boulanger, P., Letellier, L. EMBO J. (1996) [Pubmed]
  3. Binding of iron-free siderophore, a common feature of siderophore outer membrane transporters of Escherichia coli and Pseudomonas aeruginosa. Hoegy, F., Celia, H., Mislin, G.L., Vincent, M., Gallay, J., Schalk, I.J. J. Biol. Chem. (2005) [Pubmed]
  4. FhuA-mediated phage genome transfer into liposomes: a cryo-electron tomography study. Böhm, J., Lambert, O., Frangakis, A.S., Letellier, L., Baumeister, W., Rigaud, J.L. Curr. Biol. (2001) [Pubmed]
  5. The TonB-dependent ferrichrome receptor FcuA of Yersinia enterocolitica: evidence against a strict co-evolution of receptor structure and substrate specificity. Koebnik, R., Hantke, K., Braun, V. Mol. Microbiol. (1993) [Pubmed]
  6. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Ferguson, A.D., Hofmann, E., Coulton, J.W., Diederichs, K., Welte, W. Science (1998) [Pubmed]
  7. Conversion of the FhuA transport protein into a diffusion channel through the outer membrane of Escherichia coli. Killmann, H., Benz, R., Braun, V. EMBO J. (1993) [Pubmed]
  8. DNA delivery by phage as a strategy for encapsulating toroidal condensates of arbitrary size into liposomes. Lambert, O., Letellier, L., Gelbart, W.M., Rigaud, J.L. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  9. The beta-barrel domain of FhuADelta5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli. Braun, M., Killmann, H., Braun, V. Mol. Microbiol. (1999) [Pubmed]
  10. Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane. Boulanger, P., le Maire, M., Bonhivers, M., Dubois, S., Desmadril, M., Letellier, L. Biochemistry (1996) [Pubmed]
  11. Genetic insertion and exposure of a reporter epitope in the ferrichrome-iron receptor of Escherichia coli K-12. Moeck, G.S., Bazzaz, B.S., Gras, M.F., Ravi, T.S., Ratcliffe, M.J., Coulton, J.W. J. Bacteriol. (1994) [Pubmed]
  12. Analysis of the Erwinia chrysanthemi ferrichrysobactin receptor gene: resemblance to the Escherichia coli fepA-fes bidirectional promoter region and homology with hydroxamate receptors. Sauvage, C., Franza, T., Expert, D. J. Bacteriol. (1996) [Pubmed]
  13. Deletion of the proline-rich region of TonB disrupts formation of a 2:1 complex with FhuA, an outer membrane receptor of Escherichia coli. Khursigara, C.M., De Crescenzo, G., Pawelek, P.D., Coulton, J.W. Protein Sci. (2005) [Pubmed]
  14. Dimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coli. Koedding, J., Howard, P., Kaufmann, L., Polzer, P., Lustig, A., Welte, W. J. Biol. Chem. (2004) [Pubmed]
  15. Ferrioxamine uptake in Yersinia enterocolitica: characterization of the receptor protein FoxA. Bäumler, A.J., Hantke, K. Mol. Microbiol. (1992) [Pubmed]
  16. Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains. Eisenhauer, H.A., Shames, S., Pawelek, P.D., Coulton, J.W. J. Biol. Chem. (2005) [Pubmed]
  17. Cell envelope signaling in Escherichia coli. Ligand binding to the ferrichrome-iron receptor fhua promotes interaction with the energy-transducing protein TonB. Moeck, G.S., Coulton, J.W., Postle, K. J. Biol. Chem. (1997) [Pubmed]
  18. Exchangeability of N termini in the ligand-gated porins of Escherichia coli. Scott, D.C., Cao, Z., Qi, Z., Bauler, M., Igo, J.D., Newton, S.M., Klebba, P.E. J. Biol. Chem. (2001) [Pubmed]
  19. Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli K-12. Moeck, G.S., Tawa, P., Xiang, H., Ismail, A.A., Turnbull, J.L., Coulton, J.W. Mol. Microbiol. (1996) [Pubmed]
  20. Phage display reveals multiple contact sites between FhuA, an outer membrane receptor of Escherichia coli, and TonB. Carter, D.M., Gagnon, J.N., Damlaj, M., Mandava, S., Makowski, L., Rodi, D.J., Pawelek, P.D., Coulton, J.W. J. Mol. Biol. (2006) [Pubmed]
  21. Characterization of a high-affinity complex between the bacterial outer membrane protein FhuA and the phage T5 protein pb5. Plançon, L., Janmot, C., le Maire, M., Desmadril, M., Bonhivers, M., Letellier, L., Boulanger, P. J. Mol. Biol. (2002) [Pubmed]
  22. The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides. Sean Peacock, R., Weljie, A.M., Peter Howard, S., Price, F.D., Vogel, H.J. J. Mol. Biol. (2005) [Pubmed]
WikiGenes - Universities