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  1. 原著論文

Reaction mechanism of tetrathionate hydrolysis based on the crystal structure of tetrathionate hydrolase from Acidithiobacillus ferrooxidans

https://repo.qst.go.jp/records/80836
https://repo.qst.go.jp/records/80836
3beb47f7-865e-4353-bc5d-3176e0ff1b06
Item type 学術雑誌論文 / Journal Article(1)
公開日 2020-10-29
タイトル
タイトル Reaction mechanism of tetrathionate hydrolysis based on the crystal structure of tetrathionate hydrolase from Acidithiobacillus ferrooxidans
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
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Kanao, Tadayoshi

× Kanao, Tadayoshi

WEKO 1006095

Kanao, Tadayoshi

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Hase, Naruki

× Hase, Naruki

WEKO 1006096

Hase, Naruki

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Nakayama, Hisayuki

× Nakayama, Hisayuki

WEKO 1006097

Nakayama, Hisayuki

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Yoshida, Kyoya

× Yoshida, Kyoya

WEKO 1006098

Yoshida, Kyoya

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Nishiura, Kazumi

× Nishiura, Kazumi

WEKO 1006099

Nishiura, Kazumi

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Kosaka, Megumi

× Kosaka, Megumi

WEKO 1006100

Kosaka, Megumi

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Kamimura, Kazuo

× Kamimura, Kazuo

WEKO 1006101

Kamimura, Kazuo

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Hirano, Yuu

× Hirano, Yuu

WEKO 1006102

Hirano, Yuu

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Tamada, Taro

× Tamada, Taro

WEKO 1006103

Tamada, Taro

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Yuu, Hirano

× Yuu, Hirano

WEKO 1006104

en Yuu, Hirano

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Taro, Tamada

× Taro, Tamada

WEKO 1006105

en Taro, Tamada

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抄録
内容記述タイプ Abstract
内容記述 Tetrathionate hydrolase (4THase) plays an important role in dissimilatory sulfur oxidation in the acidophilic iron- and sulfur-oxidizing bacterium Acidithiobacillus ferrooxidans. The structure of recombinant 4THase from A. ferrooxidans (Af-Tth) was determined by X-ray crystallography to a resolution of 1.95 Å. Af-Tth is a homodimer, and its monomer structure exhibits an eight-bladed β-propeller motif. Two insertion loops participate in dimerization, and one loop forms a cavity with the β-propeller region. We observed unexplained electron densities in this cavity of the substrate-soaked structure. The anomalous difference map generated using diffraction data collected at a wavelength of 1.9 Å indicated the presence of polymerized sulfur atoms. Asp325, a highly conserved residue among 4THases, was located near the polymerized sulfur atoms. 4THase activity was completely abolished in the site-specific Af-Tth D325N variant, suggesting that Asp325 plays a crucial role in the first step of tetrathionate hydrolysis. Considering that the Af-Tth reaction occurs only under acidic pH, Asp325 acts as an acid for the tetrathionate hydrolysis reaction. The polymerized sulfur atoms in the active site cavity may represent the intermediate product in the subsequent step.
書誌情報 Protein Science

巻 30, 号 2, p. 328-338, 発行日 2020-10
出版者
出版者 Wiley
ISSN
収録物識別子タイプ ISSN
収録物識別子 0961-8368
DOI
識別子タイプ DOI
関連識別子 10.1002/pro.3984
関連サイト
識別子タイプ DOI
関連識別子 https://doi.org/10.1002/pro.3984
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