FhuA barrel-cork hybrids are active transporters and receptors

Journal of Bacteriology
Helmut KillmannV Braun

Abstract

The crystal structure of Escherichia coli FhuA reveals a beta-barrel domain that is closed by a globular cork domain. It has been assumed that the proton motive force of the cytoplasmic membrane through the interaction of the TonB protein with the TonB box of the cork opens the FhuA channel. Yet, deletion of the cork results in an FhuA derivative, FhuADelta5-160, that still displays TonB-dependent substrate transport and phage receptor activity. To investigate this unexpected finding further, we constructed FhuADelta5-160 derivatives of FhuA proteins from Salmonella paratyphi B, Salmonella enterica serovar Typhimurium, and Pantoea agglomerans. The FhuADelta5-160 proteins inserted correctly into the outer membrane, and with the exception of the P. agglomerans protein, transported ferrichrome and albomycin. FhuA hybrids consisting of the beta-barrel of one strain and the cork of another strain were active and showed higher TonB-dependent ferrichrome transport rates than the corkless derivatives. Exceptions were the E. coli beta-barrel/Salmonella serovar Typhimurium cork hybrid protein and the Salmonella serovar Typhimurium beta-barrel/P. agglomerans cork hybrid protein, both of which were less active than the beta-barrels alone. ...Continue Reading

References

Jul 1, 1978·Journal of Bacteriology·K Hantke, V Braun
Oct 5, 1990·Journal of Molecular Biology·S F AltschulD J Lipman
Feb 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·S Tabor, C C Richardson
Jan 1, 1984·Molecular & General Genetics : MGG·T OlschlägerV Braun
Jun 1, 1996·Journal of Bacteriology·J O SolbiatiR A Salomón
Sep 15, 1999·Proceedings of the National Academy of Sciences of the United States of America·N Cadieux, R J Kadner
Mar 4, 2000·Nature Structural Biology·H J MerianosD S Cafiso
Jun 13, 2000·Protein Science : a Publication of the Protein Society·A D FergusonW Welte

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Citations

Nov 9, 2002·Biochimie·Volkmar BraunKlaus Hantke
Apr 6, 2002·Current Opinion in Microbiology·Volkmar Braun, Michael Braun
Oct 18, 2002·European Journal of Biochemistry·Michael BraunVolkmar Braun
Sep 10, 2002·Journal of Bacteriology·Hema L Vakharia, Kathleen Postle
Oct 26, 2002·Journal of Bacteriology·Christopher D Kenney, Cynthia Nau Cornelissen
Mar 2, 2002·Journal of Bacteriology·Qixun Zhao, Keith Poole
Sep 2, 2003·Journal of Bacteriology·Michael BraunVolkmar Braun
Jul 3, 2004·Journal of Bacteriology·Franziska Endriss, Volkmar Braun
May 3, 2013·BMC Microbiology·María Fernanda PomaresPaula A Vincent
Jan 13, 2016·FEMS Microbiology Letters·Juliano Bertozzi SilvaDominic Sauvageau
Nov 24, 2004·Biochemical and Biophysical Research Communications·Augusto BellomioRicardo N Farías
Jun 28, 2003·FEMS Microbiology Reviews·Simon C AndrewsFrancisco Rodríguez-Quiñones
Oct 19, 2004·Annual Review of Microbiology·Cécile Wandersman, Philippe Delepelaire
Apr 22, 2017·Nature Communications·Samuel J HickmanDavid J Brockwell
Nov 26, 2013·Applied and Environmental Microbiology·Minsik KimSangryeol Ryu
Nov 13, 2002·Microbiology·Helmut KillmannVolkmar Braun

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