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Rossmann-Fold Methyltransferases: Taking a “β-Turn” around Their Cofactor, S-Adenosylmethionine
https://oist.repo.nii.ac.jp/records/1050
https://oist.repo.nii.ac.jp/records/1050e65b1953-2686-4855-86c6-f4f63f077abe
名前 / ファイル | ライセンス | アクション |
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ACS_Biochemistry_Manuscript (801.3 kB)
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ACS_Biochemistry_Manuscript_Supplementary (3.5 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2019-08-05 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Rossmann-Fold Methyltransferases: Taking a “β-Turn” around Their Cofactor, S-Adenosylmethionine | |||||
言語 | ||||||
言語 | eng | |||||
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(英) |
Chouhan, Bhanu Pratap Singh
× Chouhan, Bhanu Pratap Singh× Maimaiti, Shayida× Gade, Madhuri× Laurino, Paola |
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書誌情報 |
en : Biochemistry 巻 58, 号 3, p. 166-170, 発行日 2018-11-08 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Methyltransferases (MTases) are superfamilies of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (SAM), a nucleoside-based cofactor, to a wide variety of substrates such as DNA, RNA, proteins, small molecules, and lipids. Depending upon their structural features, the MTases can be further classified into different classes; we consider exclusively the largest class of MTases, the Rossmann-fold MTases. It has been shown that the nucleoside cofactor-binding Rossmann enzymes, particularly the nicotinamide adenine dinucleotide (NAD)-, flavin adenine dinucleotide (FAD)-, and SAM-binding MTases enzymes, share common binding motifs that include a Gly-rich loop region that interacts with the cofactor and a highly conserved acidic residue (Asp/Glu) that interacts with the ribose moiety of the cofactor. Here, we observe that the Gly-rich loop region of the Rossmann MTases adapts a specific type II′ β-turn in the proximity of the cofactor (<4 Å), and it appears to be a key feature of these superfamilies. Additionally, we demonstrate that the conservation of this β-turn could play a critical role in the enzyme–cofactor interaction, thereby shedding new light on the structural conformation of the Gly-rich loop region from Rossmann MTases. | |||||
出版者 | ||||||
出版者 | American Chemical Society | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0006-2960 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1520-4995 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/30406995 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.1021/acs.biochem.8b00994 | |||||
権利 | ||||||
権利情報 | © 2018 American Chemical Society | |||||
権利 | ||||||
権利情報 | This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.biochem.8b00994. | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://pubs.acs.org/doi/10.1021/acs.biochem.8b00994 | |||||
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 |