A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation.

A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation.
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DOI:
10.1038/nsmb.1770
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发表时间:
2010-03
影响因子:
16.8
通讯作者:
--
中科院分区:
生物学1区
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--
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ATP结合盒(ABC)转运蛋白是一种跨细胞膜转运多种底物的膜蛋白。在这里,我们提出了三个结构特征的ABC转运蛋白的复合物形成的动力学:BtuCD维生素B12进口商和MetNI D/L-蛋氨酸进口商从大肠杆菌,和流感嗜血杆菌Hi 1470/1金属螯合进口商,与他们的同源结合蛋白。与其他ABC导入剂类似,MetNI与其结合蛋白以低亲和力(Kd ~ 10-4 M)相互作用。相比之下,BtuCD-F和Hi 1470/1-2形成稳定的高亲和力复合物(Kd分别约为10-13和10-9 M)。在BtuCD-F中,维生素B12使复合物解离速率加快约107倍,ATP具有额外的去稳定作用。本文所述的研究结果突出了BtuCD-F和可能的Hi 1470/1-2与更好表征的麦芽糖和相关ABC转运系统之间的实质性机制差异,表明该大蛋白质超家族中存在相当大的机制多样性。
ATP binding cassette (ABC) transporters are integral membrane proteins that translocate a diverse array of substrates across cell membranes. We present here the dynamics of complex formation of three structurally characterized ABC transporters: the BtuCD vitamin B12 importer and MetNI D/L-methionine importer from Escherichia coli, and the Haemophilus influenzae Hi1470/1 metal-chelate importer, with their cognate binding proteins. Similar to other ABC importers, MetNI interacts with its binding protein with low affinity (Kd ~ 10-4 M). In contrast, BtuCD-F and Hi1470/1-2 form stable, high affinity complexes (Kd ~ 10-13 and 10-9 M, respectively). In BtuCD-F, vitamin B12 accelerates complex dissociation rate ~107-fold, with ATP having an additional destabilizing effect. The findings presented here highlight substantial mechanistic differences between BtuCD-F, and likely Hi1470/1-2, and the better characterized maltose and related ABC transport systems, indicating considerable mechanistic diversity within this large protein super-family.
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