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Structural basis for the substrate recognition of aminoglycoside 7′′-phosphotransferase-Ia from Streptomyces hygroscopicus
http://hdl.handle.net/2241/00159545
http://hdl.handle.net/2241/0015954512093cf4-5616-46df-9e51-155768a79559
| 名前 / ファイル | ライセンス | アクション |
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ActaCF_75-9_electronic reprint.pdf (1.8 MB)
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| Item type | アイテムタイプJ(1) | |||||||||||||||||||||
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| 公開日 | 2020-02-06 | |||||||||||||||||||||
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| タイトル | Structural basis for the substrate recognition of aminoglycoside 7′′-phosphotransferase-Ia from Streptomyces hygroscopicus | |||||||||||||||||||||
| 言語 | ||||||||||||||||||||||
| 言語 | eng | |||||||||||||||||||||
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| 資源タイプ | journal article | |||||||||||||||||||||
| 著者 |
NAKAMURA Akira
× NAKAMURA Akira
× Takenoya Mihoko
× Shimamura Tatsuro
× Yamanaka Ryuji
× Adachi Yuya
× Ito Shinsaku
× Sasaki Yasuyuki
× Yajima Shunsuke
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| 著者情報 | ||||||||||||||||||||||
| 所属・氏名 | 生命環境系; 中村, 顕; ナカムラ, アキラ; NAKAMURA, Akira | |||||||||||||||||||||
| 研究者総覧URL | http://trios.tsukuba.ac.jp/researcher/0000001202 | |||||||||||||||||||||
| 抄録 | ||||||||||||||||||||||
| 内容記述 | Hygromycin B (HygB) is one of the aminoglycoside antibiotics and it is widely used as a reagent in molecular-biology experiments. Two kinases are known to inactivate HygB through phosphorylation: aminoglycoside 7′′-phosphotransferase-Ia [APH(7′′)-Ia] from Streptomyces hygroscopicus and aminoglycoside 4-phosphotransferase-Ia [APH(4)-Ia] from Escherichia coli. They phosphorylate the hydroxyl groups at positions 7′′ and 4 of the HygB molecule respectively. Previously the crystal structure of APH(4)-Ia was reported as a ternary complex with HygB and 5′-adenylyl-β,γ-imidodiphosphate (AMP-PNP). To investigate the differences in the substrate-recognition mechanism between APH(7′′)-Ia and APH(4)-Ia the crystal structure of APH(7′′)-Ia complexed with HygB is reported. The overall structure of APH(7′′)-Ia is similar to those of other aminoglycoside phosphotransferases including APH(4)-Ia and consists of an N-terminal lobe (N-lobe) and a C-terminal lobe (C-lobe). The latter also comprises a core and a helical domain. Accordingly the APH(7′′)-Ia and APH(4)-Ia structures fit globally when the structures are superposed at three catalytically important conserved residues His Asp and Asn in the Brenner motif which is conserved in aminoglycoside phosphotransferases as well as in eukaryotic protein kinases. On the other hand the phosphorylated hydroxyl groups of HygB in both structures come close to the Asp residue and the HygB molecules in each structure lie in opposite directions. These molecules were held by the helical domain in the C-lobe which exhibited structural differences between the two kinases. Furthermore based on the crystal structures of APH(7′′)-Ia and APH(4)-Ia some mutated residues in their thermostable mutants reported previously were located at the same positions in the two enzymes. | |||||||||||||||||||||
| 書誌情報 |
en : Acta Crystallographica Section F Structural Biology Communications 巻 75, 号 9, p. 599-607, 発行日 2019-09 |
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| 収録物識別子 | 2053-230X | |||||||||||||||||||||
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| アクセス権 | open access | |||||||||||||||||||||
| 権利情報 | ||||||||||||||||||||||
| 権利情報 | © 2019 International Union of Crystallography | |||||||||||||||||||||
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| 出版者 | International Union of Crystallography | |||||||||||||||||||||
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| 出版タイプ | VoR | |||||||||||||||||||||
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| 関連タイプ | isIdenticalTo | |||||||||||||||||||||
| 関連識別子 | https://doi.org/10.1107/S2053230X19011105 | |||||||||||||||||||||
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| 関連識別子 | 31475927 | |||||||||||||||||||||
