Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.

Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.
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DOI:
10.1038/srep07299
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发表时间:
2014-12-03
期刊:
影响因子:
4.6
通讯作者:
Nureki O
Nureki O
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Kumazaki K;Kishimoto T;Furukawa A;Mori H;Tanaka Y;Dohmae N;Ishitani R;Tsukazaki T;Nureki O

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细菌YidC是一种进化上保守的膜蛋白,其功能是与Sec易位子合作的膜蛋白伴侣,并作为膜蛋白的独立插入酶。在革兰氏阴性细菌中,YidC的跨膜和周质区域与Sec蛋白相互作用,形成用于Sec依赖性膜蛋白整合的多蛋白复合物。在这里,我们报告了全长大肠杆菌YidC的晶体结构。该结构揭示了由五个跨膜螺旋形成的亲水性凹槽是YidC的保守结构特征,与来自嗜盐芽孢杆菌的先前YidC结构相比,其缺乏周质结构域。底物或Sec蛋白接触位点的结构映射表明YidC作为伴侣和插入酶功能的沟的重要性,并提供了对多蛋白复合物的结构洞察。
Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In Gram-negative bacteria, the transmembrane and periplasmic regions of YidC interact with the Sec proteins, forming a multi-protein complex for Sec-dependent membrane protein integration. Here, we report the crystal structure of full-length Escherichia coli YidC. The structure reveals that a hydrophilic groove, formed by five transmembrane helices, is a conserved structural feature of YidC, as compared to the previous YidC structure from Bacillus halodurans, which lacks a periplasmic domain. Structural mapping of the substrate- or Sec protein-contact sites suggested the importance of the groove for the YidC functions as a chaperone and an insertase, and provided structural insight into the multi-protein complex.
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影响因子: 4.8
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