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Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation.

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タイトル: Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation.
著者: Yamazawa, Ryuji / Nakajima, Yoshitaka / Mushiake, Karin / Yoshimoto, Tadashi / Ito, Kiyoshi
発行日: 2011年 6月
出版者: Oxford University Press
引用: Journal of Biochemistry, 149(6), pp.701-712; 2011
抄録: 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.
キーワード: conformational change / crystal structure / serine dehydrogenase / short-chain dehydrogenase/reductase family / substrate recognition
URI: http://hdl.handle.net/10069/27411
ISSN: 0021924X
DOI: 10.1093/jb/mvr024
PubMed ID: 21349860
権利: © The Authors 2011. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved. / 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.
資料タイプ: Journal Article
原稿種類: author
出現コレクション:050 学術雑誌論文

引用URI : http://hdl.handle.net/10069/27411



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