+データを開く
-基本情報
登録情報 | データベース: SASBDB / ID: SASDAZ6 |
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試料 | CyaY-dimer and IscS-dimer complex
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機能・相同性 | 機能・相同性情報 IscS-TusA complex / oxazole or thiazole biosynthetic process / tRNA 4-thiouridine biosynthesis / IscS-IscU complex / sulfur compound transport / selenocysteine catabolic process / sulfurtransferase complex / sulfur carrier activity / detection of UV / selenocysteine lyase activity ...IscS-TusA complex / oxazole or thiazole biosynthetic process / tRNA 4-thiouridine biosynthesis / IscS-IscU complex / sulfur compound transport / selenocysteine catabolic process / sulfurtransferase complex / sulfur carrier activity / detection of UV / selenocysteine lyase activity / tRNA wobble position uridine thiolation / L-cysteine desulfurase complex / iron chaperone activity / cysteine desulfurase / cysteine desulfurase activity / L-cysteine catabolic process / thiamine biosynthetic process / [2Fe-2S] cluster assembly / iron-sulfur cluster assembly / ferroxidase activity / ferric iron binding / ferrous iron binding / 2 iron, 2 sulfur cluster binding / pyridoxal phosphate binding / intracellular iron ion homeostasis / metal ion binding / cytoplasm / cytosol 類似検索 - 分子機能 |
生物種 | Escherichia coli (大腸菌) |
引用 | ジャーナル: Nat Commun / 年: 2010 タイトル: Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. 著者: Filippo Prischi / Petr V Konarev / Clara Iannuzzi / Chiara Pastore / Salvatore Adinolfi / Stephen R Martin / Dmitri I Svergun / Annalisa Pastore / 要旨: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin ...Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin to iron-sulphur cluster assembly through interactions with the two central components of this machinery: desulphurase Nfs1/IscS and the scaffold protein Isu/IscU. In this study, we use a combination of biophysical methods to define the structural bases of the interaction of CyaY (the bacterial orthologue of frataxin) with the IscS/IscU complex. We show that CyaY binds IscS as a monomer in a pocket between the active site and the IscS dimer interface. Recognition does not require iron and occurs through electrostatic interactions of complementary charged residues. Mutations at the complex interface affect the rates of enzymatic cluster formation. CyaY binding strengthens the affinity of the IscS/IscU complex. Our data suggest a new paradigm for understanding the role of frataxin as a regulator of IscS functions. |
登録者 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-モデル
モデル #231 | タイプ: atomic / ソフトウェア: SASREF / ダミー原子の半径: 1.90 A / 対称性: P2 / カイ2乗値: 8.1796 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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モデル #232 | タイプ: dummy / ソフトウェア: DAMMIF / ダミー原子の半径: 3.90 A / 対称性: P2 / カイ2乗値: 1.1664 Omokage検索でこの集合体の類似形状データを探す (詳細) |
-試料
試料 | 名称: CyaY-dimer and IscS-dimer complex / 試料濃度: 2.50-5.00 / Entity id: 135 / 139 |
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バッファ | 名称: Tris-HCl / 濃度: 20.00 mM / pH: 8 コメント: errous ammonium sulphate was added to reach a 1:1:2 CyaY/IscS/Fe molar ratio under aerobic condition 組成: 50 mM NaCl, 10 mM β-mercaptoethanol and ferrous ammonium sulphate (as CyaY binds both Fe(II) and Fe(III), ferrous ammonium sulphate was added to reach a 1:1:2 CyaY/IscS/Fe molar ratio under aerobic conditions) |
要素 #135 | タイプ: protein / 記述: Cysteine desulfurase IscS / 分子量: 43.597 / 分子数: 2 / 由来: Escherichia coli / 参照: UniProt: P0A6B7 配列: KLPIYLDYSA TTPVDPRVAE KMMQFMTMDG TFGNPASRSH RFGWQAEEAV DIARNQIADL VGADPREIVF TSGATESDNL AIKGAANFYQ KKGKHIITSK TEHKAVLDTC RQLEREGFEV TYLAPQRNGI IDLKELEAAM RDDTILVSIM HVNNEIGVVQ DIAAIGEMCR ...配列: KLPIYLDYSA TTPVDPRVAE KMMQFMTMDG TFGNPASRSH RFGWQAEEAV DIARNQIADL VGADPREIVF TSGATESDNL AIKGAANFYQ KKGKHIITSK TEHKAVLDTC RQLEREGFEV TYLAPQRNGI IDLKELEAAM RDDTILVSIM HVNNEIGVVQ DIAAIGEMCR ARGIIYHVDA TQSVGKLPID LSQLKVDLMS FSGHKIYGPK GIGALYVRRK PRVRIEAQMH GGGHERGMRS GTLPVHQIVG MGEAYRIAKE EMATEMERLR GLRNRLWNGI KDIEEVYLNG DLEHGAPNIL NVSFNYVEGE SLIMALKDLA VSSGSACTSA SLEPSYVLRA LGLNDELAHS SIRFSLGRFT TEEEIDYTIE LVRKSIGRLR DLSPLWEMYK Q |
要素 #139 | タイプ: protein / 記述: Protein CyaY / 分子量: 12.231 / 分子数: 2 / 由来: Escherichia coli / 参照: UniProt: P27838 配列: MNDSEFHRLA DQLWLTIEER LDDWDGDSDI DCEINGGVLT ITFENGSKII INRQEPLHQV WLATKQGGYH FDLKGDEWIC DRSGETFWDL LEQAATQQAG ETVSFR |
-実験情報
ビーム | 設備名称: DORIS III X33 / 地域: Hamburg / 国: Germany / 形状: 0.6 / 線源: X-ray synchrotron / 波長: 0.15 Å / スペクトロメータ・検出器間距離: 2.7 mm | ||||||||||||||||||
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検出器 | 名称: Pilatus 1M-W / Pixsize x: 0.172 mm | ||||||||||||||||||
スキャン | タイトル: sy / 測定日: 2009年11月5日 / 保管温度: 15 °C / セル温度: 15 °C / 照射時間: 30 sec. / フレーム数: 4 / 単位: 1/nm /
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距離分布関数 P(R) | ソフトウェア P(R): GNOM 4.5a / ポイント数: 379 /
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結果 | D max: 10.87 / カーブのタイプ: single_conc / Standard: bovin serum albumin コメント: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich’s ataxia. Independent reports have ...コメント: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich’s ataxia. Independent reports have linked frataxin to iron–sulphur cluster assembly through interactions with the two central components of this machinery: desulphurase Nfs1/IscS and the scaffold protein Isu/IscU. In this study, we use a combination of biophysical methods to define the structural bases of the interaction of CyaY (the bacterial orthologue of frataxin) with the IscS/IscU complex. We show that CyaY binds IscS as a monomer in a pocket between the active site and the IscS dimer interface. Recognition does not require iron and occurs through electrostatic interactions of complementary charged residues. Mutations at the complex interface affect the rates of enzymatic cluster formation. CyaY binding strengthens the affinity of the IscS/IscU complex. Our data suggest a new paradigm for understanding the role of frataxin as a regulator of IscS functions.
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