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
影响因子:
4.6
通讯作者:
Nureki O
中科院分区:
文献类型:
--
作者:
Kumazaki K;Kishimoto T;Furukawa A;Mori H;Tanaka Y;Dohmae N;Ishitani R;Tsukazaki T;Nureki O
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:
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通讯作者:
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DOI:
10.1107/s0907444909052925
发表时间:
2010-02
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
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作者:
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通讯作者:
Zwart PH