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Catalytic mechanism and evolutional characteristics of thioredoxin from Halobacterium salinarum NRC-1
https://repo.qst.go.jp/records/78401
https://repo.qst.go.jp/records/7840154902fe1-970f-49ef-8fcb-52aceb2b6f3e
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2019-08-05 | |||||
| タイトル | ||||||
| タイトル | Catalytic mechanism and evolutional characteristics of thioredoxin from Halobacterium salinarum 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_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 |
Arai, Shigeki
× Arai, Shigeki× Shibazaki, Chie× Shimizu, Rumi× Adachi, Motoyasu× Ishibashi, Matsujiro× Tokunaga, Hiroko× Tokunaga, Masao× Shigeki, Arai× Chie, Shibazaki× Rumi, Shimizu× Motoyasu, Adachi |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | AbstractThioredoxin (TRX) is an important antioxidant against oxidative stress. TRX from Halobacterium salinarum NRC-1 (HsTRX-A), which has the highest acidic residue content ([Asp + Glu] / [Arg + Lys + His] = 9.0) among known TRXs, was chosen to elucidate a catalytic mechanism and evolutionary characteristics associated with haloadaptation. X-ray crystallographic analysis revealed that the main chain structure of HsTRX-A is similar to those of homologous TRXs; e.g., root-mean-square deviations for Cα atoms were <2.3 Å for the extant archaeal TRXs and <1.5 Å for the resurrected Precambrian TRXs. The density of negative charges at the molecular surface (0.0035 Å-2) and the structural flexibility of the long N-terminal coil (Arg1–Pro16) of HsTRX-A were higher than those of homologous TRXs and should improve solubility and haloadaptivity. Circular dichroism measurement indicated that the structure of HsTRX-A is highly flexible and that a high salt concentration (~4 M NaCl) is required for structural stabilization. A unique water network was located near the active-site residues (Cys47 and Cys50) in HsTRX-A, which may enhance the proton transfer required for reduction of substrates under a high-salt environment. A structural inspection of TRXs revealed that helix α1 in TRXs elongated during evolution from LACA-TRX (the last archaeal common ancestor TRX) to extant archaeal TRXs, including HsTRX-A. These observations offer insights into molecular evolution for haloadaptation and potential applications in halophilic protein-related biotechnology. | |||||
| 書誌情報 |
Acta Crystallographica section D 巻 76, 号 1, p. 73-84, 発行日 2020-01 |
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| 出版者 | ||||||
| 出版者 | International Union of Crystallography | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 2059-7983 | |||||
| PubMed番号 | ||||||
| 識別子タイプ | PMID | |||||
| 関連識別子 | 31909745 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1107/S2059798319015894 | |||||
| 関連サイト | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | http://scripts.iucr.org/cgi-bin/paper?S2059798319015894 | |||||
