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基本情報
登録情報 | データベース: EMDB / ID: EMD-4324 | |||||||||
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タイトル | 26S proteasome, s6 state | |||||||||
![]() | 26S proteasome in state S6 | |||||||||
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![]() | 26S proteasome / AAA+ ATPase / HYDROLASE | |||||||||
機能・相同性 | ![]() SAGA complex localization to transcription regulatory region / Metalloprotease DUBs / proteasome regulatory particle assembly / proteasome storage granule assembly / transcription export complex 2 / protein deneddylation / peroxisome fission / maintenance of DNA trinucleotide repeats / filamentous growth / COP9 signalosome ...SAGA complex localization to transcription regulatory region / Metalloprotease DUBs / proteasome regulatory particle assembly / proteasome storage granule assembly / transcription export complex 2 / protein deneddylation / peroxisome fission / maintenance of DNA trinucleotide repeats / filamentous growth / COP9 signalosome / proteasome regulatory particle / protein-containing complex localization / proteasome-activating activity / mitochondrial fission / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / metal-dependent deubiquitinase activity / K48-linked polyubiquitin modification-dependent protein binding / proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / 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 / nonfunctional rRNA decay / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / 3-deoxy-7-phosphoheptulonate synthase / 3-deoxy-7-phosphoheptulonate synthase activity / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / peptide catabolic process / KEAP1-NFE2L2 pathway / Neddylation / proteasome binding / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / regulation of protein catabolic process / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / polyubiquitin modification-dependent protein binding / protein deubiquitination / positive regulation of RNA polymerase II transcription preinitiation complex assembly / chorismate biosynthetic process / Ub-specific processing proteases / proteasome endopeptidase complex / endopeptidase activator activity / proteasome core complex, beta-subunit complex / proteasome assembly / aromatic amino acid family biosynthetic process / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / mRNA export from nucleus / enzyme regulator activity / amino acid biosynthetic process / ERAD pathway / Neutrophil degranulation / protein folding chaperone / proteasome complex / ubiquitin binding / double-strand break repair via homologous recombination / nucleotide-excision repair / positive regulation of transcription elongation by RNA polymerase II / metallopeptidase activity / positive regulation of protein catabolic process / peroxisome / ubiquitin-dependent protein catabolic process / protein-macromolecule adaptor activity / endopeptidase activity / molecular adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / regulation of cell cycle / chromatin remodeling / protein domain specific 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 / metal ion binding / identical protein binding / nucleus / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | ![]() ![]() | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 6.1 Å | |||||||||
![]() | Eisele MR / Reed RG | |||||||||
![]() | ![]() 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 |
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構造ビューア | EMマップ: ![]() ![]() ![]() |
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ダウンロードとリンク
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マップデータ | ![]() | 202.4 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 49.5 KB 49.5 KB | 表示 表示 | ![]() |
画像 | ![]() | 53 KB | ||
Filedesc metadata | ![]() | 13.1 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 271.1 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 270.2 KB | 表示 | |
XML形式データ | ![]() | 6.7 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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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 | 26S proteasome in state S6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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
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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'-TRIPHOSPHATE
+分子 #35: MAGNESIUM ION
+分子 #36: 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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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.4 |
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凍結 | 凍結剤: ETHANE-PROPANE |
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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: ![]() |
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 |
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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: 6.1 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 184988 |
初期 角度割当 | タイプ: PROJECTION MATCHING |
最終 角度割当 | タイプ: PROJECTION MATCHING |