Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF
抄録
Protein secretion mediated by SecYEG translocon and SecA ATPase is enhanced by membrane-embedded SecDF by using proton motive force. A previous structural study of SecDF indicated that it comprises 12 transmembrane helices that can conduct protons and three periplasmic domains, which form at least two characterized transition states, termed the F and I forms. We report the structures of full-length SecDF in I form at 2.6- to 2.8-A resolution. The structures revealed that SecDF in I form can generate a tunnel that penetrates the transmembrane region and functions as a proton pathway regulated by a conserved Asp residue of the transmembrane region. In one crystal structure, periplasmic cavity interacts with a molecule, potentially polyethylene glycol, which may mimic a substrate peptide. This study provides structural insights into the Sec protein translocation that allows future analyses to develop a more detailed working model for SecDF.
収録刊行物
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- Cell Reports
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Cell Reports 19 (5), 895-901, 2017-05-02
Cell Press
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詳細情報 詳細情報について
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- CRID
- 1050577309352789248
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- NII論文ID
- 120006226309
- 120006353868
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- ISSN
- 22111247
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- HANDLE
- 10061/11714
- 2433/227558
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- Crossref
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