The assembly of β-barrel outer membrane proteins.

The assembly of β-barrel outer membrane proteins.
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DOI:
10.1016/j.mib.2021.01.009
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发表时间:
2021-04
影响因子:
5.4
通讯作者:
Kahne D
Kahne D
中科院分区:
生物学2区
文献类型:
--
作者:
Tomasek D;Kahne D

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革兰氏阴性菌、线粒体和叶绿体的外膜含有β-桶整合膜蛋白。五蛋白β桶组装机(BAM)加速了这些蛋白质的折叠和膜整合。该机器的中心组件BamA包含β桶结构域,该结构域可以采用横向开放状态,其N端和C端β链未配对。最近,已经开发了在BAM复合物上捕获β-桶折叠中间体的策略。生化和结构的研究提供了支持的模型,其中基板组装在侧向开口的BamA。在该模型中,BamA的N端β链通过氢键结合捕获底物的C端β链,以允许它们定向折叠并随后释放到膜中。
The outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts contain β-barrel integral membrane proteins. The five-protein β-barrel assembly machine (Bam) accelerates the folding and membrane integration of these proteins. The central component of the machine, BamA, contains a β-barrel domain that can adopt a lateral-open state with its N- and C-terminal β-strands unpaired. Recently, strategies have been developed to capture β-barrel folding intermediates on the Bam complex. Biochemical and structural studies provide support for a model in which substrates assemble at the lateral opening of BamA. In this model, the N-terminal β-strand of BamA captures the C-terminal β-strand of substrates by hydrogen bonding to allow their directional folding and subsequent release into the membrane.
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