ABC transporters: one, two or four extracytoplasmic substrate-binding sites?

被引:150
作者
van der Heide, T [1 ]
Poolman, B [1 ]
机构
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Biochem, NL-9747 AG Groningen, Netherlands
关键词
D O I
10.1093/embo-reports/kvf201
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
Two families of ATP-binding cassette (ABC) transporters in which one or two extracytoplasmic substrate-binding domains are fused to either the N- or C-terminus of the translocator protein have been detected. This suggests that two, or even four, substrate-binding sites may function in the ABC transporter complex. This domain organization in ABC transporters, widely represented among microorganisms, raises new possibilities for how the substrate-binding protein(s) (SBPs) might interact with the translocator. One appealing hypothesis is that multiple substrate-binding sites in proximity to the entry site of the translocation pore enhance the transport capacity. We also discuss the implications of multiple substrate-binding sites in close proximity to the translocator in terms of broadened substrate specificity and possible cooperative interactions between SBPs and the translocator.
引用
收藏
页码:938 / 943
页数:6
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