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J Mol Biol. 2008 May 9;378(4):840-51. doi: 10.1016/j.jmb.2008.03.044. Epub 2008 Mar 28.

Modulation by substrates of the interaction between the HasR outer membrane receptor and its specific TonB-like protein, HasB.

Author information

1
Département de Biologie Structurale et de Chimie, Unité de Résonance Magnétique Nucléaire des Biomolécules, Institut Pasteur, CNRS URA 2185 28, rue du Dr. Roux, 75724 Paris Cedex 15, France.

Abstract

TonB is a cytoplasmic membrane protein required for active transport of various essential substrates such as heme and iron siderophores through the outer membrane receptors of Gram-negative bacteria. This protein spans the periplasm, contacts outer membrane transporters by its C-terminal domain, and transduces energy from the protonmotive force to the transporters. The TonB box, a relatively conserved sequence localized on the periplasmic side of the transporters, has been shown to directly contact TonB. While Serratia marcescens TonB functions with various transporters, HasB, a TonB-like protein, is dedicated to the HasR transporter. HasR acquires heme either freely or via an extracellular heme carrier, the hemophore HasA, that binds to HasR and delivers heme to the transporter. Here, we study the interaction of HasR with a HasB C-terminal domain and compare it with that obtained with a TonB C-terminal fragment. Analysis of the thermodynamic parameters reveals that the interaction mode of HasR with HasB differs from that with TonB, the difference explaining the functional specificity of HasB for HasR. We also demonstrate that the presence of the substrate on the extracellular face of the transporter modifies, via enthalpy-entropy compensation, the interaction with HasB on the periplasmic face. The transmitted signal depends on the nature of the substrate. While the presence of heme on the transporter modifies only slightly the nature of interactions involved between HasR and HasB, hemophore binding on the transporter dramatically changes the interactions and seems to locally stabilize some structural motifs. In both cases, the HasR TonB box is the target for those modifications.

PMID:
18402979
DOI:
10.1016/j.jmb.2008.03.044
[Indexed for MEDLINE]

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