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基本情報
| 登録情報 | データベース: SASBDB / ID: SASDCZ9 |
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試料 | Glyceraldehyde-3-phosphate dehydrogenase from C. reinhardtii
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| 機能・相同性 | 機能・相同性情報酸化還元酵素; アルデヒドまたはケトンに対し酸化酵素として働く; NAD又はNADPを用いる / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / glucose metabolic process / NAD binding / NADP binding 類似検索 - 分子機能 |
| 生物種 | ![]() |
引用 | ジャーナル: J Mol Biol / 年: 2018タイトル: Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase. 著者: Hélène Launay / Patrick Barré / Carine Puppo / Yizhi Zhang / Stéphanie Maneville / Brigitte Gontero / Véronique Receveur-Bréchot / ![]() 要旨: Among intrinsically disordered proteins, conditionally disordered proteins undergo dramatic structural disorder rearrangements upon environmental changes and/or post-translational modifications that ...Among intrinsically disordered proteins, conditionally disordered proteins undergo dramatic structural disorder rearrangements upon environmental changes and/or post-translational modifications that directly modulate their function. Quantifying the dynamics of these fluctuating proteins is extremely challenging but paramount to understanding the regulation of their function. The chloroplast protein CP12 is a model of such proteins and acts as a redox switch by formation/disruption of its two disulfide bridges. It regulates the Calvin cycle by forming, in oxidized conditions, a supramolecular complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and then phosphoribulokinase. In this complex, both enzymes are inactive. The highly dynamic nature of CP12 has so far hindered structural characterization explaining its mode of action. Thanks to a synergistic combination of small-angle X-ray scattering, nuclear magnetic resonance and circular dichroism that drove the molecular modeling of structural ensembles, we deciphered the structural behavior of Chlamydomonas reinhardtii oxidized CP12 alone and in the presence of GAPDH. Contrary to sequence-based structural predictions, the N-terminal region is unstable, oscillates at the ms timescale between helical and random conformations, and is connected through a disordered linker to its C-terminus, which forms a stable helical turn. Upon binding to GAPDH, oxidized CP12 undergoes an induced unfolding of its N-terminus. This phenomenon called cryptic disorder contributes to decrease the entropy cost and explains CP12 unusual high affinity for its partners. |
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構造の表示
| 構造ビューア | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
-モデル
| モデル #1699 | ![]() タイプ: atomic / ダミー原子の半径: 1.90 A / カイ2乗値: 8.543929 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 #1700 | ![]() タイプ: atomic / ダミー原子の半径: 1.90 A / カイ2乗値: 8.415801 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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試料
試料 | 名称: Glyceraldehyde-3-phosphate dehydrogenase from C. reinhardtii 試料濃度: 23 mg/ml |
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| バッファ | 名称: 30 mM Tris, 4 mM EDTA, 100 µM NAD, 5 mM free cysteine pH: 7.9 |
| 要素 #911 | 名称: GAPDH / タイプ: protein / 記述: Glyceraldehyde-3-phosphate dehydrogenase / 分子量: 36.881 / 分子数: 4 / 由来: Chlamydomonas reinhardtii / 参照: UniProt: A8HP84 配列: EKKIRVAING FGRIGRNFLR CWHGRQNTLL DVVAINDSGG VKQASHLLKY DSTLGTFAAD VKIVDDSHIS VDGKQIKIVS SRDPLQLPWK EMNIDLVIEG TGVFIDKVGA GKHIQAGASK VLITAPAKDK DIPTFVVGVN EGDYKHEYPI ISNASCTTNC LAPFVKVLEQ ...配列: EKKIRVAING FGRIGRNFLR CWHGRQNTLL DVVAINDSGG VKQASHLLKY DSTLGTFAAD VKIVDDSHIS VDGKQIKIVS SRDPLQLPWK EMNIDLVIEG TGVFIDKVGA GKHIQAGASK VLITAPAKDK DIPTFVVGVN EGDYKHEYPI ISNASCTTNC LAPFVKVLEQ KFGIVKGTMT TTHSYTGDQR LLDASHRDLR RARAAALNIV PTTTGAAKAV SLVLPSLKGK LNGIALRVPT PTVSVVDLVV QVEKKTFAEE VNAAFREAAN GPMKGVLHVE DAPLVSIDFK CTDQSTSIDA SLTMVMGDDM VKVVAWYDNE WGYSQRVVDL AEVTAKKWVA |
-実験情報
| ビーム | 設備名称: SOLEIL SWING / 地域: Saint-Aubin / 国: France / 線源: X-ray synchrotron / 波長: 0.1033 Å / スペクトロメータ・検出器間距離: 1.817 mm | ||||||||||||||||||||||||||||||||||||
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| 検出器 | 名称: AVIEX / タイプ: CCD | ||||||||||||||||||||||||||||||||||||
| スキャン | 測定日: 2011年2月7日 / 保管温度: 15 °C / セル温度: 20 °C / 照射時間: 1 sec. / フレーム数: 250 / 単位: 1/A /
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