TY - JOUR
T1 - The substrate-binding protein in bacterial ABC transporters
T2 - Dissecting roles in the evolution of substrate specificity
AU - Maqbool, Abbas
AU - Horler, Richard S P
AU - Muller, Axel
AU - Wilkinson, Anthony J.
AU - Wilson, Keith S.
AU - Thomas, Gavin H.
PY - 2015/10/9
Y1 - 2015/10/9
N2 - 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.
AB - 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.
KW - Adenosine 5′-triphosphate-binding cassette (ABC) transporter
KW - Evolution
KW - Substrate specificity
KW - Substratebinding protein (SBP)
UR - http://www.scopus.com/inward/record.url?scp=84947246951&partnerID=8YFLogxK
U2 - 10.1042/BST20150135
DO - 10.1042/BST20150135
M3 - Article
AN - SCOPUS:84947246951
SN - 0300-5127
VL - 43
SP - 1011
EP - 1017
JO - Biochemical Society transactions
JF - Biochemical Society transactions
IS - 5
ER -