Recognition of iron-free siderophores by TonB-dependent iron transporters.

TonB-dependent iron transporters reside in the outer membranes of Gram-negative bacteria, transporting ferric-complexes into the periplasm by a mechanism requiring proton motive force and an integral inner membrane complex, TonB-ExbB-ExbD. Certain TonB-dependent transporters contain an additional do...

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Main Authors: Schalk, I, Yue, W, Buchanan, S
Format: Journal article
Language:English
Published: 2004
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author Schalk, I
Yue, W
Buchanan, S
author_facet Schalk, I
Yue, W
Buchanan, S
author_sort Schalk, I
collection OXFORD
description TonB-dependent iron transporters reside in the outer membranes of Gram-negative bacteria, transporting ferric-complexes into the periplasm by a mechanism requiring proton motive force and an integral inner membrane complex, TonB-ExbB-ExbD. Certain TonB-dependent transporters contain an additional domain at the N-terminus, which interacts with an inner membrane regulatory protein and a cytoplasmic sigma factor to induce transcription of iron transport genes when a ferric-ligand is bound at the extracellular surface of the transporter. Transport of the ferric-ligand is apparently not necessary for transcription induction. Recent biophysical and crystallographic experiments have shown that this subclass of TonB-dependent iron transporters can bind iron-free ligands, whereas only the ferric-ligands are transported into the periplasm. This review focuses on the ligand binding properties of these transporters and includes a discussion of the biological function of the additional domain, the mechanism of transcription induction and the mechanism of ferric-ligand transport.
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spelling oxford-uuid:66f0c921-7949-4688-afce-240139d530b72022-03-26T18:34:57ZRecognition of iron-free siderophores by TonB-dependent iron transporters.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:66f0c921-7949-4688-afce-240139d530b7EnglishSymplectic Elements at Oxford2004Schalk, IYue, WBuchanan, STonB-dependent iron transporters reside in the outer membranes of Gram-negative bacteria, transporting ferric-complexes into the periplasm by a mechanism requiring proton motive force and an integral inner membrane complex, TonB-ExbB-ExbD. Certain TonB-dependent transporters contain an additional domain at the N-terminus, which interacts with an inner membrane regulatory protein and a cytoplasmic sigma factor to induce transcription of iron transport genes when a ferric-ligand is bound at the extracellular surface of the transporter. Transport of the ferric-ligand is apparently not necessary for transcription induction. Recent biophysical and crystallographic experiments have shown that this subclass of TonB-dependent iron transporters can bind iron-free ligands, whereas only the ferric-ligands are transported into the periplasm. This review focuses on the ligand binding properties of these transporters and includes a discussion of the biological function of the additional domain, the mechanism of transcription induction and the mechanism of ferric-ligand transport.
spellingShingle Schalk, I
Yue, W
Buchanan, S
Recognition of iron-free siderophores by TonB-dependent iron transporters.
title Recognition of iron-free siderophores by TonB-dependent iron transporters.
title_full Recognition of iron-free siderophores by TonB-dependent iron transporters.
title_fullStr Recognition of iron-free siderophores by TonB-dependent iron transporters.
title_full_unstemmed Recognition of iron-free siderophores by TonB-dependent iron transporters.
title_short Recognition of iron-free siderophores by TonB-dependent iron transporters.
title_sort recognition of iron free siderophores by tonb dependent iron transporters
work_keys_str_mv AT schalki recognitionofironfreesiderophoresbytonbdependentirontransporters
AT yuew recognitionofironfreesiderophoresbytonbdependentirontransporters
AT buchanans recognitionofironfreesiderophoresbytonbdependentirontransporters