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Conformational variation of the translocon enhancing chaperone SecDF
http://hdl.handle.net/10061/9863
http://hdl.handle.net/10061/98630bb59e73-4d10-444e-b371-8b4fdfcc6056
名前 / ファイル | ライセンス | アクション |
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fulltext (849.2 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2015-05-26 | |||||
タイトル | ||||||
タイトル | Conformational variation of the translocon enhancing chaperone SecDF | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Conformational change | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | EM | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | SecDF | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Single particle analysis | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Translocon | |||||
資源タイプ | ||||||
資源タイプ | journal article | |||||
アクセス権 | ||||||
アクセス権 | open access | |||||
著者 |
Mio, Kazuhiro
× Mio, Kazuhiro× Tsukazaki, Tomoya× Mori, Hiroyuki× Kawata, Masaaki× Moriya, Toshio× Sasaki, Yoshikazu× Ishitani, Ryuichiro× Ito, Koreaki× Nureki, Osamu× Sato, Chikara |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | The Sec translocon facilitates transportation of newly synthesized polypeptides from the cytoplasm to the lumen/periplasm across the phospholipid membrane. Although the polypeptide-conducting machinery is formed by the SecYEG-SecA complex in bacteria, its transportation efficiency is markedly enhanced by SecDF. A previous study suggested that SecDF assumes at least two conformations differing by a 120° rotation in the spatial orientation of the P1 head subdomain to the rigid base, and that the conformational dynamics plays a critical role in polypeptide translocation. Here we addressed this hypothesis by analyzing the 3D structure of SecDF using electron tomography and single particle reconstruction. Reconstruction of wt SecDF showed two major conformations; one resembles the crystal structure of full-length SecDF (F-form structure), while the other is similar to the hypothetical structural variant based on the crystal structure of the isolated P1 domain (I-form structure). The transmembrane domain of the I-form structure has a scissor like cleft open to the periplasmic side. We also report the structure of a double cysteine mutant designed to constrain SecDF to the I-form. This reconstruction has a protrusion at the periplasmic end that nicely fits the orientation of P1 in the I-from. These results provide firm evidence for the occurrence of the I-form in solution and support the proposed F- to I-transition of wt SecDF during polypeptide translocation. | |||||
書誌情報 |
en : Journal of Structural and Functional Genomics 巻 15, 号 3, p. 107-115, 発行日 2014-09-01 |
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出版者 | ||||||
出版者 | Springer Netherlands | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1345-711X | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | https://doi.org/10.1007/s10969-013-9168-4 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA12022720 | |||||
権利 | ||||||
権利情報 | 出版社許諾条件により、本文は2015年9月2日以降に公開 | |||||
権利 | ||||||
権利情報 | c Springer International Publishing AG, Part of Springer Science+Business Media | |||||
著者版フラグ | ||||||
出版タイプ | AM |