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PMID: 19179287 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter.

Mulligan C, Geertsma ER, Severi E, Kelly DJ, Poolman B, Thomas GH

Abstract

Substrate-binding protein-dependent secondary transporters are widespread in prokaryotes and are represented most frequently by members of the tripartite ATP-independent periplasmic (TRAP) transporter family. Here, we report the membrane reconstitution of a TRAP transporter, the sialic acid-specific SiaPQM system from Haemophilus influenzae, and elucidate its mechanism of energy coupling. Uptake of sialic acid via membrane-reconstituted SiaQM depends on the presence of the sialic acid-binding protein, SiaP, and is driven by the electrochemical sodium gradient. The interaction between SiaP and SiaQM is specific as transport is not reconstituted using the orthologous sialic acid-binding protein VC1779. Importantly, the binding protein also confers directionality on the transporter, and reversal of sialic acid transport from import to export is only possible in the presence of an excess of unliganded SiaP.

MeSH Terms
Biological Transport Energy Metabolism Haemophilus influenzae/chemistry Membrane Transport Proteins/metabolism N-Acetylneuraminic Acid/metabolism Organic Anion Transporters/metabolism Protein Binding Substrate Specificity Symporters/metabolism Viral Proteins/metabolism
Chemicals
Membrane Transport Proteins Organic Anion Transporters Symporters Viral Proteins sialic acid transport proteins N-Acetylneuraminic Acid
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Mulligan Christopher
Department of Biology (Area 10), University of York, P.O. Box 373, York YO10 5YW, United Kingdom.
Geertsma Eric R
Severi Emmanuele
Kelly David J
Poolman Bert
Thomas Gavin H
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
1091-6490
Published
2009-02-10
Epub
2009-00-28
Pages
1778-83
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC2644114
Subset
IM
Grants
Biotechnology and Biological Sciences Research Council · BB/F014759/1 · United Kingdom
Corrections
ErratumIn
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