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Tripartite ATP-independent periplasmic (TRAP) transporters in bacteria and archaea

Mulligan, Christopher, Fischer, Marcus, Thomas, Gavin H (2010) Tripartite ATP-independent periplasmic (TRAP) transporters in bacteria and archaea. FEMS microbiology reviews, 35 (1). pp. 68-86. ISSN 1574-6976. (doi:10.1111/j.1574-6976.2010.00236.x) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1111/j.1574-6976.2010.00236.x

Abstract

The tripartite ATP-independent periplasmic (TRAP) transporters are the best-studied family of substrate-binding protein (SBP)-dependent secondary transporters and are ubiquitous in prokaryotes, but absent from eukaryotes. They are comprised of an SBP of the DctP or TAXI families and two integral membrane proteins of unequal sizes that form the DctQ and DctM protein families, respectively. The SBP component has a structure comprised of two domains connected by a hinge that closes upon substrate binding. In DctP-TRAP transporters, substrate binding is mediated through a conserved and specific arginine/carboxylate interaction in the SBP. While the SBP component has now been relatively well characterized, the membrane components of TRAP transporters are still poorly understood both in terms of their structure and function. We review the expanding repertoire of substrates and physiological roles for experimentally characterized TRAP transporters in bacteria and discuss mechanistic aspects of these transporters using data primarily from the sialic acid-specific TRAP transporter SiaPQM from Haemophilus influenzae, which suggest that TRAP transporters are high-affinity, Na(+)-dependent unidirectional secondary transporters.

Item Type: Article
DOI/Identification number: 10.1111/j.1574-6976.2010.00236.x
Uncontrolled keywords: tripartite ATP-independent periplasmic, TRAP transporter, sialic acid, periplasmic binding protein, extracytoplasmic solute receptor, SiaP
Subjects: Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Christopher Mulligan
Date Deposited: 10 May 2017 14:47 UTC
Last Modified: 06 Feb 2020 04:16 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/61669 (The current URI for this page, for reference purposes)
Mulligan, Christopher: https://orcid.org/0000-0001-5157-4651
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