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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/2241/00159545
12093cf4-5616-46df-9e51-155768a79559
名前 / ファイル ライセンス アクション
ActaCF_75-9_electronic ActaCF_75-9_electronic reprint.pdf (1.8 MB)
Item type アイテムタイプJ(1)
公開日 2020-02-06
タイトル
タイトル Structural basis for the substrate recognition of aminoglycoside 7′′-phosphotransferase-Ia from Streptomyces hygroscopicus
言語
言語 eng
資源タイプ
資源タイプ journal article
著者 NAKAMURA Akira

× NAKAMURA Akira

en NAKAMURA Akira

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Takenoya Mihoko

× Takenoya Mihoko

en Takenoya Mihoko

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Shimamura Tatsuro

× Shimamura Tatsuro

en Shimamura Tatsuro

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Yamanaka Ryuji

× Yamanaka Ryuji

en Yamanaka Ryuji

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Adachi Yuya

× Adachi Yuya

en Adachi Yuya

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Ito Shinsaku

× Ito Shinsaku

en Ito Shinsaku

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Sasaki Yasuyuki

× Sasaki Yasuyuki

en Sasaki Yasuyuki

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Yajima Shunsuke

× Yajima Shunsuke

en 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
PISSN
収録物識別子 2053-230X
アクセス権
アクセス権 open access
権利情報
権利情報 © 2019 International Union of Crystallography
出版者
出版者 International Union of Crystallography
出版タイプ
出版タイプ VoR
DOI
関連タイプ isIdenticalTo
関連識別子 https://doi.org/10.1107/S2053230X19011105
PMID
関連識別子 31475927
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