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Structure and dimerization of the catalytic domain of the protein phosphatase Cdc14p, a key regulator of mitotic exit in Saccharomyces cerevisiae
http://hdl.handle.net/2237/27281
http://hdl.handle.net/2237/2728107074df8-05f0-4d33-b845-629e684e2a40
名前 / ファイル | ライセンス | アクション |
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2018-01-18 | |||||
タイトル | ||||||
タイトル | Structure and dimerization of the catalytic domain of the protein phosphatase Cdc14p, a key regulator of mitotic exit in Saccharomyces cerevisiae | |||||
言語 | en | |||||
著者 |
Kobayashi, Junya
× Kobayashi, Junya× Matsuura, Yoshiyuki |
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アクセス権 | ||||||
アクセス権 | open access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
権利 | ||||||
言語 | en | |||||
権利情報 | This is the peer reviewed version of the following article: [Kobayashi, J. and Matsuura, Y. (2017), Structure and dimerization of the catalytic domain of the protein phosphatase Cdc14p, a key regulator of mitotic exit in Saccharomyces cerevisiae. Protein Science, 26: 2105–2112. doi:10.1002/pro.3244], which has been published in final form at [http://doi.org/10.1002/pro.3244]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | cell cycle | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | mitotic exit | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | protein phosphatase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Cdc14 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | dimerization | |||||
抄録 | ||||||
内容記述 | In the budding yeast Saccharomyces cerevisiae, the protein phosphatase Cdc14p orchestrates various events essential for mitotic exit. We have determined the X-ray crystal structures at 1.85 Å resolution of the catalytic domain of Cdc14p in both the apo state, and as a complex with S160-phosphorylated Swi6p peptide. Each asymmetric unit contains two Cdc14p chains arranged in an intimately associated homodimer, consistent with its oligomeric state in solution. The dimerization interface is located on the backside of the substrate-binding cleft. Structure-based mutational analyses indicate that the dimerization of Cdc14p is required for normal growth of yeast cells. | |||||
言語 | en | |||||
内容記述タイプ | Abstract | |||||
出版者 | ||||||
言語 | en | |||||
出版者 | Wiley | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプresource | http://purl.org/coar/resource_type/c_6501 | |||||
タイプ | journal article | |||||
出版タイプ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | https://doi.org/10.1002/pro.3244 | |||||
ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 0961-8368 | |||||
書誌情報 |
en : Protein Science 巻 26, 号 10, p. 2105-2112, 発行日 2017-10 |
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著者版フラグ | ||||||
値 | author | |||||
URI | ||||||
識別子 | http://doi.org/10.1002/pro.3244 | |||||
識別子タイプ | DOI | |||||
URI | ||||||
識別子 | http://hdl.handle.net/2237/27281 | |||||
識別子タイプ | HDL |