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基本情報
登録情報 | データベース: EMDB / ID: EMD-3414 | |||||||||
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タイトル | Structures of human peroxiredoxin 3 suggest self-chaperoning assembly that maintains catalytic state | |||||||||
![]() | Reconstruction of Human Peroxiredoxin3 filaments formed at pH 4 | |||||||||
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機能・相同性 | ![]() peptidyl-cysteine oxidation / alkyl hydroperoxide reductase activity / maternal placenta development / thioredoxin-dependent peroxiredoxin / myeloid cell differentiation / thioredoxin peroxidase activity / negative regulation of kinase activity / Detoxification of Reactive Oxygen Species / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / cell redox homeostasis ...peptidyl-cysteine oxidation / alkyl hydroperoxide reductase activity / maternal placenta development / thioredoxin-dependent peroxiredoxin / myeloid cell differentiation / thioredoxin peroxidase activity / negative regulation of kinase activity / Detoxification of Reactive Oxygen Species / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / cell redox homeostasis / regulation of mitochondrial membrane potential / mitochondrion organization / hydrogen peroxide catabolic process / response to hydrogen peroxide / cellular response to reactive oxygen species / positive regulation of NF-kappaB transcription factor activity / cellular response to oxidative stress / response to oxidative stress / response to lipopolysaccharide / early endosome / mitochondrial matrix / intracellular membrane-bounded organelle / positive regulation of cell population proliferation / negative regulation of apoptotic process / protein kinase binding / protein-containing complex / mitochondrion / nucleoplasm / identical protein binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | ![]() | |||||||||
手法 | らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 4.1 Å | |||||||||
![]() | Yewdall AN / Venugopal HP / Desfosses A / Abrishami V / Yosaatmadja Y / Hampton MB / Gerrard JA / Goldstone D / Mitra AK / Mazdak Radjainia M | |||||||||
![]() | ![]() タイトル: Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State. 著者: N Amy Yewdall / Hariprasad Venugopal / Ambroise Desfosses / Vahid Abrishami / Yuliana Yosaatmadja / Mark B Hampton / Juliet A Gerrard / David C Goldstone / Alok K Mitra / Mazdak Radjainia / ![]() ![]() 要旨: Peroxiredoxins are antioxidant proteins primarily responsible for detoxification of hydroperoxides in cells. On exposure to various cellular stresses, peroxiredoxins can acquire chaperone activity, ...Peroxiredoxins are antioxidant proteins primarily responsible for detoxification of hydroperoxides in cells. On exposure to various cellular stresses, peroxiredoxins can acquire chaperone activity, manifested as quaternary reorganization into a high molecular weight (HMW) form. Acidification, for example, causes dodecameric rings of human peroxiredoxin 3 (HsPrx3) to stack into long helical filaments. In this work, a 4.1-Å resolution structure of low-pH-instigated helical filaments was elucidated, showing a locally unfolded active site and partially folded C terminus. A 2.8-Å crystal structure of HsPrx3 was determined at pH 8.5 under reducing conditions, wherein dodecameric rings are arranged as a short stack, with symmetry similar to low-pH filaments. In contrast to previous observations, the crystal structure displays both a fully folded active site and ordered C terminus, suggesting that the HsPrx3 HMW form maintains catalytic activity. We propose a new role for the HMW form as a self-chaperoning assembly maintaining HsPrx3 function under stress. | |||||||||
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構造の表示
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構造ビューア | EMマップ: ![]() ![]() ![]() |
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マップデータ | ![]() | 17.3 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 8.6 KB 8.6 KB | 表示 表示 | ![]() |
画像 | ![]() | 730.6 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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リンク
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Reconstruction of Human Peroxiredoxin3 filaments formed at pH 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.372 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
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試料の構成要素
-全体 : Human peroxiredoxin-3 filament
全体 | 名称: Human peroxiredoxin-3 filament |
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要素 |
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-超分子 #1000: Human peroxiredoxin-3 filament
超分子 | 名称: Human peroxiredoxin-3 filament / タイプ: sample / ID: 1000 / Number unique components: 1 |
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-分子 #1: Peroxiredoxin-3
分子 | 名称: Peroxiredoxin-3 / タイプ: protein_or_peptide / ID: 1 / 組換発現: Yes |
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由来(天然) | 生物種: ![]() |
組換発現 | 生物種: ![]() ![]() |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | らせん対称体再構成法 |
試料の集合状態 | filament |
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試料調製
緩衝液 | 詳細: 20 mM HEPES, 75 mM NaCl |
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グリッド | 詳細: Quantifoil R2/2 |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / 装置: FEI VITROBOT MARK IV |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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日付 | 2014年10月1日 |
撮影 | カテゴリ: CCD フィルム・検出器のモデル: FEI FALCON II (4k x 4k) 実像数: 769 / 平均電子線量: 42 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.0 mm |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
詳細 | SPRING |
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最終 再構成 | 想定した対称性 - らせんパラメータ - Δz: 42.6 Å 想定した対称性 - らせんパラメータ - ΔΦ: 8.7 ° 想定した対称性 - らせんパラメータ - 軸対称性: D6 (2回x6回 2面回転対称) 解像度のタイプ: BY AUTHOR / 解像度: 4.1 Å / 解像度の算出法: OTHER / ソフトウェア - 名称: SPRING |