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

被引:0
|
作者
Oded Lewinson
Allen T Lee
Kaspar P Locher
Douglas C Rees
机构
[1] Division of Chemistry and Chemical Engineering,
[2] Howard Hughes Medical Institute,undefined
[3] California Institute of Technology,undefined
[4] Institute of Molecular Biology and Biophysics,undefined
来源
Nature Structural & Molecular Biology | 2010年 / 17卷
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摘要
ABC transporters move substrates across the membrane. The substrate is often delivered by a binding protein. Functional analysis of the bacterial BtuCD-F system now reveals a distinct mechanism for substrate delivery different from other ABC transporters, whereby the binding protein associates with the transporter in the absence of substrate, and substrate or ATP binding destabilize the complex.
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页码:332 / 338
页数:6
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