+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-4321 | |||||||||
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タイトル | 26S proteasome, s3 state | |||||||||
マップデータ | 26S proteasome state s3 | |||||||||
試料 |
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キーワード | 26S proteasome / AAA+ ATPase / hydrolase | |||||||||
機能・相同性 | 機能・相同性情報 SAGA complex localization to transcription regulatory region / Metalloprotease DUBs / peroxisome fission / proteasome storage granule assembly / transcription export complex 2 / proteasome regulatory particle assembly / protein deneddylation / maintenance of DNA trinucleotide repeats / filamentous growth / COP9 signalosome ...SAGA complex localization to transcription regulatory region / Metalloprotease DUBs / peroxisome fission / proteasome storage granule assembly / transcription export complex 2 / proteasome regulatory particle assembly / protein deneddylation / maintenance of DNA trinucleotide repeats / filamentous growth / COP9 signalosome / proteasome regulatory particle / cytosolic proteasome complex / proteasome regulatory particle, lid subcomplex / protein-containing complex localization / proteasome-activating activity / mitochondrial fission / proteasome regulatory particle, base subcomplex / metal-dependent deubiquitinase activity / nonfunctional rRNA decay / K48-linked polyubiquitin modification-dependent protein binding / proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / 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 / peptide catabolic process / KEAP1-NFE2L2 pathway / proteasome binding / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / regulation of protein catabolic process / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / polyubiquitin modification-dependent protein binding / endopeptidase activator activity / protein deubiquitination / proteasome assembly / positive regulation of RNA polymerase II transcription preinitiation complex assembly / 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 / ERAD pathway / protein folding chaperone / Neutrophil degranulation / proteasome complex / ubiquitin binding / nucleotide-excision repair / positive regulation of transcription elongation by RNA polymerase II / double-strand break repair via homologous recombination / positive regulation of protein catabolic process / metallopeptidase activity / peroxisome / 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 / chromatin remodeling / protein domain specific binding / mRNA binding / ubiquitin protein ligase binding / endoplasmic reticulum membrane / structural molecule activity / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / mitochondrion / ATP binding / identical protein binding / nucleus / metal ion binding / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (パン酵母) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 5.4 Å | |||||||||
データ登録者 | Eisele MR / Reed RG | |||||||||
引用 | ジャーナル: Cell Rep / 年: 2018 タイトル: Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating. 著者: Markus R Eisele / Randi G Reed / Till Rudack / Andreas Schweitzer / Florian Beck / Istvan Nagy / Günter Pfeifer / Jürgen M Plitzko / Wolfgang Baumeister / Robert J Tomko / Eri Sakata / 要旨: The proteasome is the central protease for intracellular protein breakdown. Coordinated binding and hydrolysis of ATP by the six proteasomal ATPase subunits induces conformational changes that drive ...The proteasome is the central protease for intracellular protein breakdown. Coordinated binding and hydrolysis of ATP by the six proteasomal ATPase subunits induces conformational changes that drive the unfolding and translocation of substrates into the proteolytic 20S core particle for degradation. Here, we combine genetic and biochemical approaches with cryo-electron microscopy and integrative modeling to dissect the relationship between individual nucleotide binding events and proteasome conformational dynamics. We demonstrate unique impacts of ATP binding by individual ATPases on the proteasome conformational distribution and report two conformational states of the proteasome suggestive of a rotary ATP hydrolysis mechanism. These structures, coupled with functional analyses, reveal key roles for the ATPases Rpt1 and Rpt6 in gating substrate entry into the core particle. This deepened knowledge of proteasome conformational dynamics reveals key elements of intersubunit communication within the proteasome and clarifies the regulation of substrate entry into the proteolytic chamber. | |||||||||
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_4321.map.gz | 202.6 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-4321-v30.xml emd-4321.xml | 49.5 KB 49.5 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_4321.png | 53.3 KB | ||
Filedesc metadata | emd-4321.cif.gz | 13.1 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-4321 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4321 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_4321_validation.pdf.gz | 264.8 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_4321_full_validation.pdf.gz | 263.9 KB | 表示 | |
XML形式データ | emd_4321_validation.xml.gz | 6.8 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4321 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4321 | 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_4321.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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注釈 | 26S proteasome state s3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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
+超分子 #1: 26S proteasome
+分子 #1: Proteasome subunit alpha type-1
+分子 #2: Proteasome subunit alpha type-2
+分子 #3: Proteasome subunit alpha type-3
+分子 #4: Proteasome subunit alpha type-4
+分子 #5: Proteasome subunit alpha type-5
+分子 #6: Proteasome subunit alpha type-6
+分子 #7: Probable proteasome subunit alpha type-7
+分子 #8: Proteasome subunit beta type-1
+分子 #9: Proteasome subunit beta type-2
+分子 #10: Proteasome subunit beta type-3
+分子 #11: Proteasome subunit beta type-4
+分子 #12: Proteasome subunit beta type-5
+分子 #13: Proteasome subunit beta type-6
+分子 #14: Proteasome subunit beta type-7
+分子 #15: 26S proteasome regulatory subunit RPN10
+分子 #16: Ubiquitin carboxyl-terminal hydrolase RPN11
+分子 #17: 26S proteasome regulatory subunit RPN12
+分子 #18: 26S proteasome regulatory subunit RPN13
+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: ADENOSINE-5'-DIPHOSPHATE
+分子 #35: MAGNESIUM ION
+分子 #36: ADENOSINE-5'-TRIPHOSPHATE
-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
緩衝液 | pH: 7.4 |
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凍結 | 凍結剤: ETHANE-PROPANE |
-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 |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
-画像解析
初期モデル | モデルのタイプ: PDB ENTRY PDBモデル - PDB ID: |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 5.4 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 292279 |
初期 角度割当 | タイプ: PROJECTION MATCHING |
最終 角度割当 | タイプ: PROJECTION MATCHING |