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The substrate-binding protein in bacterial ABC transporters: dissecting roles in the evolution of substrate specificity
- 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.
- Subjects :
- Models, Molecular
chemistry.chemical_classification
Binding Sites
Bacteria
Protein subunit
Monosaccharides
Tripartite ATP-independent periplasmic transporter
ATP-binding cassette transporter
Plasma protein binding
Biology
Biological Evolution
Biochemistry
Bacterial cell structure
Protein Structure, Tertiary
Amino acid
Adenosine Triphosphate
Bacterial Proteins
chemistry
ATP-Binding Cassette Transporters
Binding site
Protein Binding
ATP-binding domain of ABC transporters
Subjects
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