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

被引:111
作者
Maqbool, Abbas [1 ]
Horler, Richard S. P. [1 ]
Muller, Axel [2 ]
Wilkinson, Anthony J. [2 ]
Wilson, Keith S. [2 ]
Thomas, Gavin H. [1 ]
机构
[1] Univ York, Dept Biol, York Y010 5YW, N Yorkshire, England
[2] Univ York, Dept Chem, York Struct Biol Lab, York Y010 5YW, N Yorkshire, England
基金
英国生物技术与生命科学研究理事会;
关键词
adenosine 5 ' triphosphate-binding cassette (ABC) transporter; evolution; substratebinding protein (SBP); substrate specificity; X-RAY-STRUCTURE; ESCHERICHIA-COLI; PEPTIDE-BINDING; CRYSTAL-STRUCTURES; NICKEL; OPPA; RECEPTOR; NIKA; PURIFICATION; TRIPEPTIDE;
D O I
10.1042/BST20150135
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1011 / 1017
页数:7
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