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Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation.
http://hdl.handle.net/10069/27411
http://hdl.handle.net/10069/274117c63a2dc-8132-434f-b26e-39dba2572b10
名前 / ファイル | ライセンス | アクション |
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JouBio149_701.pdf (1.1 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2012-07-01 | |||||
タイトル | ||||||
タイトル | Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation. | |||||
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 | crystal structure | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | serine dehydrogenase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | short-chain dehydrogenase/reductase family | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | substrate recognition | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Yamazawa, Ryuji
× Yamazawa, Ryuji× Nakajima, Yoshitaka× Mushiake, Karin× Yoshimoto, Tadashi× Ito, Kiyoshi |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Serine dehydrogenase from Escherichia coli is a homotetrameric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) family. This enzyme catalyses the NADP(+)-dependent oxidation of serine to 2-aminomalonate semialdehyde. The enzyme shows a stereospecificity for β-(3S)-hydroxy acid as a substrate; however, no stereospecificity was observed at the α-carbon. The structures of the ligand-free SerDH and SerDH-NADP(+)-phosphate complex were determined at 1.9 and 2.7 Å resolutions, respectively. The overall structure, including the catalytic tetrad of Asn106, Ser134, Tyr147 and Lys151, shows obvious relationships with other members of the SDR family. The structure of the substrate-binding loop and that of the C-terminal region were disordered in the ligand-free enzyme, whereas these structures were clearly defined in the SerDH-NADP(+) complex as a closed form. Interestingly, the C-terminal region was protruded from the main body and it formed an anti-parallel β-sheet with another C-terminal region on the subunit that is diagonally opposite to that in the tetramer. It is revealed that the C-terminal region possesses the important roles in substrate binding through the stabilization of the substrate-binding loop in the closed form complex. The roles of the C-terminal region along with those of the residues involved in substrate recognition were studied by site-directed mutagenesis. | |||||
書誌情報 |
Journal of Biochemistry 巻 149, 号 6, p. 701-712, 発行日 2011-06 |
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出版者 | ||||||
出版者 | Oxford University Press | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0021924X | |||||
EISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 17562651 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00694073 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | 21349860 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1093/jb/mvr024 | |||||
権利 | ||||||
権利情報 | © The Authors 2011. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved. | |||||
権利 | ||||||
権利情報 | This is a pre-copy-editing, author-produced PDF of an article accepted for publication in Journal of Biochemistry following peer review. The definitive publisher-authenticated version Journal of Biochemistry, 149(6), pp.701-712; 2011 is available online at: http://dx.doi.org/10.1093/jb/mvr024. | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Journal of Biochemistry, 149(6), pp.701-712; 2011 |