NDLI: Differential substrate-induced signaling through the TonB-dependent transporter BtuB

Content Provider	PubMed Central
Author	Cadieux, Nathalie Phan, Phu G. Cafiso, David S. Kadner, Robert J.
Copyright Year	2003
Abstract	The BtuB transporter mediates high-affinity binding and TonB-dependent active transport of vitamin B12 [cyanocobalamin (CNCbl)] across the outer membrane of Escherichia coli. A characteristic feature of TonB-dependent transporters is the Ton box, a conserved sequence near the N terminus and exposed to the periplasm. Crosslinking to TonB and site-directed spin labeling indicated that the Ton box of BtuB undergoes a substantial conformational transition in response to CNCbl binding, but only slight movement was seen in crystal structures. An in vivo method of detecting substrate-induced changes in the Ton box environment measured reaction of a biotin maleimide derivative with cysteine substitutions through the N-terminal region of BtuB between positions 1 and 31. The degree of maleimide labeling of different residues correlated with their accessibility in the crystal structure. Labeling of many positions was increased strongly when CNCbl was present, consistent with the undocking of this region proposed from spin-labeling analyses. The receptor-binding domain of colicin E3, which binds to BtuB competitively with CNCbl, resulted in decreased labeling. Both substrate-induced transitions occur in and beyond the Ton box and were affected by transport-uncoupling substitutions. Thus, two transport substrates that bind competitively to the extracellular face of BtuB stabilize opposite transitions of the Ton box.
Related Links	http://dx.doi.org/10.1073/pnas.1932538100
Ending Page	10693
Page Count	6
Starting Page	10688
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	19
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-09-16
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Differential substrate-induced signaling through the TonB-dependent transporter BtuB.

TonB-dependent ligand trapping in the BtuB transporter

Substrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved

Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter

Competing ligands stabilize alternate conformations of the energy coupling motif of a TonB-dependent outer membrane transporter

Coupling of calcium and substrate binding through loop alignment in the outer membrane transporter BtuB

Signal transduction pathway of TonB-dependent transporters

Interaction of a Partially Disordered Antisigma Factor with Its Partner, the Signaling Domain of the TonB-Dependent Transporter HasR

The crystal structure of the TonB-dependent transporter YncD reveals a positively charged substrate binding site

Differential substrate-induced signaling through the TonB-dependent transporter BtuB

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Differential substrate-induced signaling through the TonB-dependent transporter BtuB.

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Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter

Competing ligands stabilize alternate conformations of the energy coupling motif of a TonB-dependent outer membrane transporter

Coupling of calcium and substrate binding through loop alignment in the outer membrane transporter BtuB

Signal transduction pathway of TonB-dependent transporters

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