+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-14085 | ||||||||||||||||||
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タイトル | 26S proteasome Rpt1-RK -Ubp6-UbVS complex in the s2 state | ||||||||||||||||||
マップデータ | |||||||||||||||||||
試料 |
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機能・相同性 | 機能・相同性情報 SAGA complex localization to transcription regulatory region / transcription export complex 2 / proteasome regulatory particle assembly / maintenance of DNA trinucleotide repeats / filamentous growth / proteasome regulatory particle, lid subcomplex / proteasome-activating activity / proteasome regulatory particle, base subcomplex / proteasome core complex / Cross-presentation of soluble exogenous antigens (endosomes) ...SAGA complex localization to transcription regulatory region / transcription export complex 2 / proteasome regulatory particle assembly / maintenance of DNA trinucleotide repeats / filamentous growth / proteasome regulatory particle, lid subcomplex / proteasome-activating activity / proteasome regulatory particle, base subcomplex / proteasome core complex / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / regulation of protein catabolic process / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / proteasome assembly / protein deubiquitination / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / Ub-specific processing proteases / threonine-type endopeptidase activity / mRNA export from nucleus / enzyme regulator activity / protein folding chaperone / Neutrophil degranulation / proteasome complex / double-strand break repair via homologous recombination / metallopeptidase activity / protein-macromolecule adaptor activity / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / molecular adaptor activity / regulation of cell cycle / ubiquitin protein ligase binding / structural molecule activity / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / ATP binding / nucleus / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||||||||||||||
生物種 | Saccharomyces cerevisiae (パン酵母) / baker's yeast (パン酵母) / Homo sapiens (ヒト) | ||||||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 6.3 Å | ||||||||||||||||||
データ登録者 | Hung KYS / Klumpe S / Eisele MR / Elsasser S / Geng TT / Cheng TC / Joshi T / Rudack T / Sakata E / Finley D | ||||||||||||||||||
資金援助 | ドイツ, 5件
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引用 | ジャーナル: Nat Commun / 年: 2022 タイトル: Allosteric control of Ubp6 and the proteasome via a bidirectional switch. 著者: Ka Ying Sharon Hung / Sven Klumpe / Markus R Eisele / Suzanne Elsasser / Geng Tian / Shuangwu Sun / Jamie A Moroco / Tat Cheung Cheng / Tapan Joshi / Timo Seibel / Duco Van Dalen / Xin-Hua ...著者: Ka Ying Sharon Hung / Sven Klumpe / Markus R Eisele / Suzanne Elsasser / Geng Tian / Shuangwu Sun / Jamie A Moroco / Tat Cheung Cheng / Tapan Joshi / Timo Seibel / Duco Van Dalen / Xin-Hua Feng / Ying Lu / Huib Ovaa / John R Engen / Byung-Hoon Lee / Till Rudack / Eri Sakata / Daniel Finley / 要旨: The proteasome recognizes ubiquitinated proteins and can also edit ubiquitin marks, allowing substrates to be rejected based on ubiquitin chain topology. In yeast, editing is mediated by ...The proteasome recognizes ubiquitinated proteins and can also edit ubiquitin marks, allowing substrates to be rejected based on ubiquitin chain topology. In yeast, editing is mediated by deubiquitinating enzyme Ubp6. The proteasome activates Ubp6, whereas Ubp6 inhibits the proteasome through deubiquitination and a noncatalytic effect. Here, we report cryo-EM structures of the proteasome bound to Ubp6, based on which we identify mutants in Ubp6 and proteasome subunit Rpt1 that abrogate Ubp6 activation. The Ubp6 mutations define a conserved region that we term the ILR element. The ILR is found within the BL1 loop, which obstructs the catalytic groove in free Ubp6. Rpt1-ILR interaction opens the groove by rearranging not only BL1 but also a previously undescribed network of three interconnected active-site-blocking loops. Ubp6 activation and noncatalytic proteasome inhibition are linked in that they are eliminated by the same mutations. Ubp6 and ubiquitin together drive proteasomes into a unique conformation associated with proteasome inhibition. Thus, a multicomponent allosteric switch exerts simultaneous control over both Ubp6 and the proteasome. | ||||||||||||||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_14085.map.gz | 185 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-14085-v30.xml emd-14085.xml | 51.3 KB 51.3 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_14085.png | 110.7 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-14085 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-14085 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_14085_validation.pdf.gz | 436.6 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_14085_full_validation.pdf.gz | 436.2 KB | 表示 | |
XML形式データ | emd_14085_validation.xml.gz | 7.4 KB | 表示 | |
CIF形式データ | emd_14085_validation.cif.gz | 8.5 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-14085 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-14085 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_14085.map.gz / 形式: CCP4 / 大きさ: 216 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.38 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
-試料の構成要素
+全体 : 26S proteasome Rpt1-RK -Ubp6-UbVS complex in the s2 state
+超分子 #1: 26S proteasome Rpt1-RK -Ubp6-UbVS complex in the s2 state
+分子 #1: BJ4_G0020160.mRNA.1.CDS.1
+分子 #2: HLJ1_G0039880.mRNA.1.CDS.1
+分子 #3: BJ4_G0021480.mRNA.1.CDS.1
+分子 #4: HLJ1_G0048980.mRNA.1.CDS.1
+分子 #5: EM14S01-3B_G0035190.mRNA.1.CDS.1
+分子 #6: BJ4_G0043800.mRNA.1.CDS.1
+分子 #7: Probable proteasome subunit alpha type-7
+分子 #8: Proteasome subunit beta type-1
+分子 #9: Proteasome endopeptidase complex
+分子 #10: Proteasome endopeptidase complex
+分子 #11: Proteasome subunit beta
+分子 #12: Proteasome subunit beta type-5
+分子 #13: HLJ1_G0013750.mRNA.1.CDS.1
+分子 #14: Proteasome subunit beta type-7
+分子 #15: 26S proteasome regulatory subunit RPN10
+分子 #16: 26S proteasome regulatory subunit RPN11
+分子 #17: EM14S01-3B_G0050020.mRNA.1.CDS.1
+分子 #18: HLJ1_G0030700.mRNA.1.CDS.1
+分子 #19: 26S proteasome complex subunit SEM1
+分子 #20: 26S proteasome regulatory subunit RPN1
+分子 #21: 26S proteasome regulatory subunit RPN2
+分子 #22: 26S proteasome regulatory subunit RPN3
+分子 #23: 26S proteasome regulatory subunit RPN5
+分子 #24: 26S proteasome regulatory subunit RPN6
+分子 #25: 26S proteasome regulatory subunit RPN7
+分子 #26: 26S proteasome regulatory subunit RPN8
+分子 #27: 26S proteasome regulatory subunit RPN9
+分子 #28: 26S proteasome regulatory subunit 7 homolog
+分子 #29: 26S proteasome regulatory subunit 4 homolog
+分子 #30: 26S proteasome regulatory subunit 6B homolog
+分子 #31: 26S proteasome subunit RPT4
+分子 #32: 26S proteasome regulatory subunit 6A
+分子 #33: 26S proteasome regulatory subunit 8 homolog
+分子 #34: Ubiquitin carboxyl-terminal hydrolase
+分子 #35: Polyubiquitin-B
+分子 #36: ADENOSINE-5'-TRIPHOSPHATE
+分子 #37: MAGNESIUM ION
+分子 #38: ADENOSINE-5'-DIPHOSPHATE
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
濃度 | 1.5 mg/mL |
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緩衝液 | pH: 7.4 |
グリッド | モデル: Quantifoil R2/1 / 材質: COPPER / 前処理 - タイプ: GLOW DISCHARGE |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 277 K / 装置: FEI VITROBOT MARK IV |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 平均電子線量: 35.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 3.0 µm / 最小 デフォーカス(公称値): 1.8 µm |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
-画像解析
最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 6.3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 74842 |
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初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |