BioMetals

, Volume 22, Issue 4, pp 671–678

Structure–function relationships in the bifunctional ferrisiderophore FpvA receptor from Pseudomonas aeruginosa

Authors

    • Département Récepteurs et Protéines Membranaires, Ecole Supérieure de Biotechnologie de StrasbourgInstitut Gilbert-Laustriat UMR7175 CNRS/Université-Strasbourg I
    • Department of Biochemistry and Webster Centre for Infectious DiseasesUniversity of Otago
  • David Cobessi
    • Département Récepteurs et Protéines Membranaires, Ecole Supérieure de Biotechnologie de StrasbourgInstitut Gilbert-Laustriat UMR7175 CNRS/Université-Strasbourg I
Review Paper

DOI: 10.1007/s10534-008-9203-2

Cite this article as:
Schalk, I.J., Lamont, I.L. & Cobessi, D. Biometals (2009) 22: 671. doi:10.1007/s10534-008-9203-2

Abstract

FpvA is the primary outer membrane transporter required for iron acquisition via the siderophore pyoverdine (Pvd) in Pseudomonas aeruginosa. FpvA, like other ferrisiderophore transporters, consists of a membrane-spanning β-barrel occluded by a plug domain. The β-strands of the barrel are connected by large extracellular loops and periplasmic turns. Like some other TonB-dependent transporters, FpvA has a periplasmic domain involved in a signalling cascade that regulates expression of genes required for ferrisiderophore transport. Here, the structures of FpvA in different loading states are analysed in light of mutagenesis data. This analysis highlights the roles of different protein domains in Pvd-Fe uptake and the signalling cascade and reveals a strong correlation between Pvd-Fe transport and activation of the signalling cascade. It is likely that conclusions drawn for FpvA will be relevant to other TonB-dependent ferrisiderophore transport and signalling proteins.

Keywords

SiderophoreIron uptakeOuter membrane transporterPyoverdineFpvAStructure

Copyright information

© Springer Science+Business Media, LLC. 2009