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抄録

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.

収録刊行物

  • SCIENTIFIC REPORTS

    SCIENTIFIC REPORTS (4), 2014-12-03

    Macmillan Publishers

キーワード

各種コード

  • NII論文ID(NAID)
    120005716851
  • NII書誌ID(NCID)
    AA10703873
  • 本文言語コード
    ENG
  • 資料種別
    journal article
  • ISSN
    2045-2322
  • データ提供元
    IR 
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