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The substrate-binding protein in bacterial ABC transporters: dissecting roles in the evolution of substrate specificity

Authors :
Abbas Maqbool
Keith S. Wilson
Gavin H. Thomas
Richard S.P. Horler
Anthony J. Wilkinson
Axel Müller
Source :
Biochemical Society Transactions. 43:1011-1017
Publication Year :
2015
Publisher :
Portland Press Ltd., 2015.

Abstract

ATP-binding cassette (ABC) transporters, although being ubiquitous in biology, often feature a subunit that is limited primarily to bacteria and archaea. This subunit, the substrate-binding protein (SBP), is a key determinant of the substrate specificity and high affinity of ABC uptake systems in these organisms. Most prokaryotes have many SBP-dependent ABC transporters that recognize a broad range of ligands from metal ions to amino acids, sugars and peptides. Herein, we review the structure and function of a number of more unusual SBPs, including an ABC transporter involved in the transport of rare furanose forms of sugars and an SBP that has evolved to specifically recognize the bacterial cell wall-derived murein tripeptide (Mtp). Both these examples illustrate that subtle changes in binding-site architecture, including changes in side chains not directly involved in ligand co-ordination, can result in significant alteration of substrate range in novel and unpredictable ways.

Details

ISSN :
14708752 and 03005127
Volume :
43
Database :
OpenAIRE
Journal :
Biochemical Society Transactions
Accession number :
edsair.doi.dedup.....e106f5932a16e9bdfc2072ded42353f8
Full Text :
https://doi.org/10.1042/bst20150135