The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter
The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter
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DOI：
10.1074/jbc.m404343200
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发表时间：
2004-07-30
影响因子：
4.8
通讯作者：
Poolman, B
中科院分区：
文献类型：
--
作者：
Doeven, MK;Abele, R;Poolman, B
描述了一种具有非常宽的底物特异性的五组分寡肽ATP结合盒转运蛋白的纯化和功能重建。高亲和力肽的摄取依赖于配体底物结合蛋白OppA，其与转运体OppBCDF的相互作用具有比未配体OppA更高的亲和力。用组合肽文库进行的转运筛选揭示：（i）Opp转运蛋白对转运肽的氨基酸侧链没有选择性;（ii）可以结合OppA的任何肽都通过Opp转运，包括长达35个残基的非常长的肽;和（iii）OppA的结合特异性在很大程度上决定了总体转运选择性。
The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein OppA, which interacts with the translocator OppBCDF with higher affinity than unliganded OppA. Transport screening with combinatorial peptide libraries revealed that (i) the Opp transporter is not selective with respect to amino acid side chains of the transported peptides; (ii) any peptide that can bind to OppA is transported via Opp, including very long peptides up to 35 residues long; and (iii) the binding specificity of OppA largely determines the overall transport selectivity.