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Haloadaptation mechanism and evolutional characteristics of thioredoxin from Halobacterium NRC-1

https://repo.qst.go.jp/records/76123
https://repo.qst.go.jp/records/76123
428301be-9e4b-4f0d-8cf6-c0f2df12fe26
Item type 会議発表用資料 / Presentation(1)
公開日 2019-05-24
タイトル
タイトル Haloadaptation mechanism and evolutional characteristics of thioredoxin from Halobacterium NRC-1
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_c94f
資源タイプ conference object
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 新井, 栄揮

× 新井, 栄揮

WEKO 821484

新井, 栄揮

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柴崎, 千枝

× 柴崎, 千枝

WEKO 821485

柴崎, 千枝

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清水, 瑠美

× 清水, 瑠美

WEKO 821486

清水, 瑠美

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安達, 基泰

× 安達, 基泰

WEKO 821487

安達, 基泰

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石橋, 松二郎

× 石橋, 松二郎

WEKO 821488

石橋, 松二郎

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徳永, 廣子

× 徳永, 廣子

WEKO 821489

徳永, 廣子

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徳永, 正雄

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WEKO 821490

徳永, 正雄

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Arai, Shigeki

× Arai, Shigeki

WEKO 821491

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Shibazaki, Chie

× Shibazaki, Chie

WEKO 821492

en Shibazaki, Chie

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Shimizu, Rumi

× Shimizu, Rumi

WEKO 821493

en Shimizu, Rumi

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Adachi, Motoyasu

× Adachi, Motoyasu

WEKO 821494

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内容記述タイプ Abstract
内容記述 Thioredoxin (TRX) is an important antioxidant to resist the oxidative stress. In this study, the structure of TRX from an extreme halophilic archaea Halobacterium NRC-1 (HsTRX-A, UniProtKB: O46709) having the highest acidic residue content [(D+E)/(K+R+H)=9.0] in the known TRXs was investigated to elucidate its haloadaptation mechanism. X-ray crystallographic analysis revealed that the structure of HsTRX-A was similar to those of the extant archaeal and non-halophilic TRXs (RMSDs for Cα atoms < 2.3 Å) and the resurrected Precambrian TRXs (RMSDs for Cα atoms < 1.5 Å) [1]. Although the structure of HsTRX-A was almost conserved throughout evolution, HsTRX-A has unique properties; e.g. the high density of negative charges (0.0035 Å-2) and the long hydrophilic N-terminal region (R1-D34), both of which improve the solubility of protein. Moreover, the water network formed by four water molecules was found near the active site residues (C47 and C50), which may assist the proton transfer at the active site residues under high salt environment. These observations will be helpful to understand the haloadaptation mechanism and molecular evolution of HsTRX-A. [1] Ingles-Prieto, A. et al. (2013) Structure, 21, 1690.
会議概要(会議名, 開催地, 会期, 主催者等)
内容記述タイプ Other
内容記述 第19回日本蛋白質科学会年会・第71回日本細胞生物学会合同年次大会
発表年月日
日付 2019-06-24
日付タイプ Issued
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