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基本情報
| 登録情報 | データベース: PDB / ID: 9lun | ||||||
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| タイトル | Cryo-EM structure of Arabidopsis thaliana RGA in complex with GID1A, SLY1, and ASK2 (consensus map) | ||||||
要素 |
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キーワード | HORMONE / Gibberellin / DELLA motif / GRAS domain / Plant growth | ||||||
| 機能・相同性 | 機能・相同性情報fruit morphogenesis / gibberellin mediated signaling pathway / raffinose family oligosaccharide biosynthetic process / floral organ morphogenesis / negative regulation of trichome patterning / negative regulation of developmental vegetative growth / negative regulation of leaf development / regulation of seed dormancy process / positive regulation of gibberellic acid mediated signaling pathway / gibberellin binding ...fruit morphogenesis / gibberellin mediated signaling pathway / raffinose family oligosaccharide biosynthetic process / floral organ morphogenesis / negative regulation of trichome patterning / negative regulation of developmental vegetative growth / negative regulation of leaf development / regulation of seed dormancy process / positive regulation of gibberellic acid mediated signaling pathway / gibberellin binding / seed dormancy process / negative regulation of seed germination / negative regulation of gibberellic acid mediated signaling pathway / positive regulation of fertilization / salicylic acid mediated signaling pathway / meiotic cytokinesis / response to gibberellin / gibberellic acid mediated signaling pathway / response to ethylene / regulation of seed germination / ethylene-activated signaling pathway / jasmonic acid mediated signaling pathway / seed germination / response to far red light / hyperosmotic salinity response / 加水分解酵素 / response to auxin / response to jasmonic acid / embryo development ending in seed dormancy / auxin-activated signaling pathway / response to abscisic acid / regulation of reactive oxygen species metabolic process / plastid / SCF ubiquitin ligase complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / regulation of protein catabolic process / cullin family protein binding / response to cold / chromosome segregation / promoter-specific chromatin binding / cellular response to hypoxia / sequence-specific DNA binding / ubiquitin-dependent protein catabolic process / transcription cis-regulatory region binding / protein ubiquitination / DNA-binding transcription factor activity / hydrolase activity / positive regulation of gene expression / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / nucleus / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
| 生物種 | ![]() | ||||||
| 手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.8 Å | ||||||
データ登録者 | Islam, S. / Park, K. / Kwon, E. / Kim, D.Y. | ||||||
| 資金援助 | 1件
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引用 | ジャーナル: Mol Plant / 年: 2025タイトル: Structural insights into gibberellin-mediated DELLA protein degradation. 著者: Soyaab Islam / Kunwoong Park / Jing Xia / Eunju Kwon / Dong Young Kim / ![]() 要旨: Gibberellin promotes plant growth by downregulating DELLA proteins, which act as growth repressors. In the presence of gibberellin, the gibberellin receptor GID1 binds DELLA proteins, triggering ...Gibberellin promotes plant growth by downregulating DELLA proteins, which act as growth repressors. In the presence of gibberellin, the gibberellin receptor GID1 binds DELLA proteins, triggering their degradation through polyubiquitination by the SCF ubiquitin E3 ligase. Despite extensive studies, the molecular mechanisms by which DELLA proteins assemble with SCF to regulate plant growth remain poorly understood. Here, we present two cryo-electron microscopy structures of the Arabidopsis thaliana DELLA protein RGA in complex with GID1A and GID1A-SLY1-ASK2, respectively. Structural analyses revealed that RGA interacts with GID1A and SLY1 through nonoverlapping binding surfaces, stabilizing the proteins. This suggests that the SCF-RGA-GID1A complex assembles through a stepwise stabilization process induced by gibberellin. Furthermore, structural comparison with GRAS proteins indicates that RGA does not interact with IDD-family transcription factors when bound to SLY1, suggesting that DELLA protein binding to GID1/SLY1 and to transcription factors is mutually exclusive. These findings provide new insights into the gibberellin-mediated regulation of transcription factor activity by DELLA proteins. | ||||||
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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
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ダウンロード
| PDBx/mmCIF形式 | 9lun.cif.gz | 208.3 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb9lun.ent.gz | 159.8 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 9lun.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
| その他 | その他のダウンロード |
-検証レポート
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/lu/9lun ftp://data.pdbj.org/pub/pdb/validation_reports/lu/9lun | HTTPS FTP |
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-関連構造データ
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リンク
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集合体
| 登録構造単位 | ![]()
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要素
| #1: タンパク質 | 分子量: 64113.125 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 遺伝子: RGA, GRS, RGA1, At2g01570, F2I9.19 / 発現宿主: ![]() |
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| #2: タンパク質 | 分子量: 38808.922 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 遺伝子: GID1A, CXE10, GID1L1, At3g05120, T12H1.8 / 発現宿主: ![]() |
| #3: タンパク質 | 分子量: 17628.209 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 遺伝子: GID2, SLY1, At4g24210, T22A6.40 / 発現宿主: ![]() |
| #4: タンパク質 | 分子量: 19262.406 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 遺伝子: SKP1B, ASK2, UIP2, At5g42190, MJC20.30 / 発現宿主: ![]() |
| #5: 化合物 | ChemComp-GA3 / |
| 研究の焦点であるリガンドがあるか | Y |
| Has protein modification | N |
-実験情報
-実験
| 実験 | 手法: 電子顕微鏡法 |
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| EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
| 構成要素 | 名称: Heterotetramer of RGA, GID1A, SLY1, and ASK2 / タイプ: COMPLEX 詳細: Heterotetramer of the DELLA protein RGA, gibberellin receptor GID1A, F-box protein SLY1, and SKP1-like protein ASK2 Entity ID: #1-#4 / 由来: RECOMBINANT |
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| 分子量 | 値: 0.14 MDa / 実験値: NO |
| 由来(天然) | 生物種: ![]() |
| 由来(組換発現) | 生物種: ![]() |
| 緩衝液 | pH: 7.5 |
| 試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
| 試料支持 | グリッドの材料: COPPER / グリッドのサイズ: 300 divisions/in. / グリッドのタイプ: Quantifoil R1.2/1.3 |
| 急速凍結 | 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 293 K |
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電子顕微鏡撮影
| 実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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| 顕微鏡 | モデル: TFS KRIOS |
| 電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
| 電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2700 nm / 最小 デフォーカス(公称値): 600 nm / アライメント法: ZEMLIN TABLEAU |
| 試料ホルダ | 凍結剤: NITROGEN |
| 撮影 | 電子線照射量: 60 e/Å2 フィルム・検出器のモデル: FEI FALCON IV (4k x 4k) |
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解析
| EMソフトウェア | 名称: PHENIX / バージョン: 1.20.1_4487: / カテゴリ: モデル精密化 | ||||||||||||||||||||||||
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| CTF補正 | タイプ: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
| 粒子像の選択 | 選択した粒子像数: 2183664 | ||||||||||||||||||||||||
| 対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||||||
| 3次元再構成 | 解像度: 2.8 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 65737 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
| 拘束条件 |
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