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Structural and functional insights into thermally stable cytochrome c' from a thermophile

https://hiroshima.repo.nii.ac.jp/records/2008707
https://hiroshima.repo.nii.ac.jp/records/2008707
2dfa1169-384a-4ac9-8576-2e701a8734c8
名前 / ファイル ライセンス アクション
ProteinSci_26_737.pdf ProteinSci_26_737.pdf (664.6 KB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル Structural and functional insights into thermally stable cytochrome c' from a thermophile
言語 en
作成者 Fujii, Sotaro

× Fujii, Sotaro

en Fujii, Sotaro

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Oki, Hiroya

× Oki, Hiroya

en Oki, Hiroya

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Kawahara, Kazuki

× Kawahara, Kazuki

en Kawahara, Kazuki

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Yamane, Daisuke

× Yamane, Daisuke

en Yamane, Daisuke

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Yamanaka, Masaru

× Yamanaka, Masaru

en Yamanaka, Masaru

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Maruno, Takahiro

× Maruno, Takahiro

en Maruno, Takahiro

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Kobayashi, Yuji

× Kobayashi, Yuji

en Kobayashi, Yuji

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Masanari, Misa

× Masanari, Misa

en Masanari, Misa

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Wakai, Satoshi

× Wakai, Satoshi

en Wakai, Satoshi

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Nishihara, Hirofumi

× Nishihara, Hirofumi

en Nishihara, Hirofumi

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Ohkubo, Tadayasu

× Ohkubo, Tadayasu

en Ohkubo, Tadayasu

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Sambongi, Yoshihiro

× Sambongi, Yoshihiro

en Sambongi, Yoshihiro

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 © 2017 The Authors Protein Science published by Wiley Periodicals, Inc. on behalf of The Protein Society. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
主題
主題Scheme Other
主題 protein stability
主題
主題Scheme Other
主題 cytochrome c
主題
主題Scheme Other
主題 thermophile
主題
主題Scheme Other
主題 protein structure
主題
主題Scheme Other
主題 mutagenesis
主題
主題Scheme Other
主題 ligand-binding
内容記述
内容記述 Thermophilic Hydrogenophilus thermoluteolus cytochrome c0 (PHCP) exhibits higher thermal stability than a mesophilic counterpart, Allochromatium vinosum cytochrome c0 (AVCP), which has a homo-dimeric structure and ligand-binding ability. To understand the thermal stability mechanism and ligand-binding ability of the thermally stable PHCP protein, the crystal structure of PHCP was first determined. It formed a homo-dimeric structure, the main chain root mean square deviation (rmsd) value between PHCP and AVCP being 0.65 A ° . In the PHCP structure, six specific residues appeared to strengthen the heme-related and subunit–subunit interactions, which were not conserved in the AVCP structure. PHCP variants having altered subunit–subunit interactions were more severely destabilized than ones having altered heme-related interactions. The PHCP structure further revealed a ligand-binding channel and a penta-coordinated heme, as observed in the AVCP protein. A spectroscopic study clearly showed that some ligands were bound to the PHCP protein. It is concluded that the dimeric PHCP from the thermophile is effectively stabilized through heme-related and subunit–subunit interactions with conservation of the ligand-binding ability.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was performed under the Cooperative Research Program of the “Network Joint Research Center for Materials and Devices".
出版者
出版者 Wiley
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
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1002/pro.3120
関連情報
識別子タイプ PMID
関連識別子 28097774
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1002/pro.3120
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0961-8368
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1469-896X
開始ページ
開始ページ 737
書誌情報 Protein Science
Protein Science

巻 26, 号 4, p. 737-748, 発行日 2017-03-06
旧ID 48606
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