Document Detail


Structure, function and binding selectivity and stereoselectivity of siderophore-iron outer membrane transporters.
MedLine Citation:
PMID:  23046646     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
To get access to iron, microorganisms produce and release into their environment small organic metal chelators called siderophores. In parallel, they produce siderophore-iron outer membrane transporters (also called TonB-Dependent Transporters or TBDT) embedded in the outer membrane; these proteins actively reabsorb the siderophore loaded with iron from the extracellular medium. This active uptake requires energy in the form of the proton motive force transferred from the inner membrane to the outer membrane transporter via the inner membrane TonB complex. Siderophores produced by microorganisms are structurally very diverse with molecular weights of 150 up to 2000Da. Siderophore-iron uptake from the extracellular medium by TBDTs is a highly selective and sometimes even stereoselective process, with each siderophore having a specific TBDT. Unlike the siderophores, all TBDTs have similar structures and belong to the outer membrane β-barrel protein superfamily. The way in which the siderophore-iron complex passes through the TBDT is still unclear. In some bacteria, TBDTs are also partners of signaling cascades regulating the expression of proteins involved in siderophore biosynthesis and siderophore-iron acquisition.
Authors:
Isabelle J Schalk; Gaëtan L A Mislin; Karl Brillet
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Current topics in membranes     Volume:  69     ISSN:  1063-5823     ISO Abbreviation:  Curr Top Membr     Publication Date:  2012  
Date Detail:
Created Date:  2012-10-10     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9212591     Medline TA:  Curr Top Membr     Country:  United States    
Other Details:
Languages:  eng     Pagination:  37-66     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Inc. All rights reserved.
Affiliation:
UMR 7242, Université de Strasbourg-CNRS, ESBS, Boulevard Sébastien Brant, Strasbourg, France.
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