+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-0322 | |||||||||
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タイトル | TnaC-stalled ribosome complex with the titin I27 domain folding close to the ribosomal exit tunnel | |||||||||
マップデータ | Titin I27 domain folded at the exit of ribosomal tunnel | |||||||||
試料 |
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キーワード | Protein folding / ribosomal exit tunnel / nascent chain / titin I27 domain / RIBOSOME | |||||||||
機能・相同性 | 機能・相同性情報 positive regulation of tryptophan metabolic process / transcriptional attenuation by ribosome / sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / tryptophan catabolic process ...positive regulation of tryptophan metabolic process / transcriptional attenuation by ribosome / sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / tryptophan catabolic process / cardiac muscle tissue morphogenesis / protein kinase regulator activity / cardiac muscle hypertrophy / mitotic chromosome condensation / actinin binding / Striated Muscle Contraction / M band / I band / cardiac muscle cell development / structural constituent of muscle / sarcomere organization / stringent response / skeletal muscle thin filament assembly / striated muscle thin filament / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / cardiac muscle contraction / translational termination / striated muscle contraction / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / muscle contraction / protein kinase A signaling / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / condensed nuclear chromosome / response to reactive oxygen species / positive regulation of protein secretion / regulation of cell growth / DNA-templated transcription termination / response to radiation / Z disc / mRNA 5'-UTR binding / response to calcium ion / actin filament binding / large ribosomal subunit / Platelet degranulation / ribosome binding / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / ribosomal large subunit assembly / protein tyrosine kinase activity / cytoplasmic translation / protease binding / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / non-specific serine/threonine protein kinase / calmodulin binding / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / protein serine kinase activity / protein serine/threonine kinase activity / negative regulation of DNA-templated transcription / mRNA binding / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / protein homodimerization activity / DNA binding / RNA binding / extracellular exosome / zinc ion binding / extracellular region / ATP binding / identical protein binding / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | Escherichia coli (大腸菌) / 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: 3.2 Å | |||||||||
データ登録者 | Su T / Kudva R | |||||||||
資金援助 | スウェーデン, 1件
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引用 | ジャーナル: Proc Natl Acad Sci U S A / 年: 2018 タイトル: Folding pathway of an Ig domain is conserved on and off the ribosome. 著者: Pengfei Tian / Annette Steward / Renuka Kudva / Ting Su / Patrick J Shilling / Adrian A Nickson / Jeffrey J Hollins / Roland Beckmann / Gunnar von Heijne / Jane Clarke / Robert B Best / 要旨: Proteins that fold cotranslationally may do so in a restricted configurational space, due to the volume occupied by the ribosome. How does this environment, coupled with the close proximity of the ...Proteins that fold cotranslationally may do so in a restricted configurational space, due to the volume occupied by the ribosome. How does this environment, coupled with the close proximity of the ribosome, affect the folding pathway of a protein? Previous studies have shown that the cotranslational folding process for many proteins, including small, single domains, is directly affected by the ribosome. Here, we investigate the cotranslational folding of an all-β Ig domain, titin I27. Using an arrest peptide-based assay and structural studies by cryo-EM, we show that I27 folds in the mouth of the ribosome exit tunnel. Simulations that use a kinetic model for the force dependence of escape from arrest accurately predict the fraction of folded protein as a function of length. We used these simulations to probe the folding pathway on and off the ribosome. Our simulations-which also reproduce experiments on mutant forms of I27-show that I27 folds, while still sequestered in the mouth of the ribosome exit tunnel, by essentially the same pathway as free I27, with only subtle shifts of critical contacts from the C to the N terminus. | |||||||||
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_0322.map.gz | 182.6 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-0322-v30.xml emd-0322.xml | 55.7 KB 55.7 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_0322_fsc.xml | 13.2 KB | 表示 | FSCデータファイル |
画像 | emd_0322.png | 181.7 KB | ||
Filedesc metadata | emd-0322.cif.gz | 11.2 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-0322 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0322 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_0322_validation.pdf.gz | 554.2 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_0322_full_validation.pdf.gz | 553.7 KB | 表示 | |
XML形式データ | emd_0322_validation.xml.gz | 13.3 KB | 表示 | |
CIF形式データ | emd_0322_validation.cif.gz | 18.1 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0322 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0322 | 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_0322.map.gz / 形式: CCP4 / 大きさ: 196.4 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Titin I27 domain folded at the exit of ribosomal tunnel | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 1.06 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 : TnaC-stalled ribosome complex with the titin I27 domain folding c...
+超分子 #1: TnaC-stalled ribosome complex with the titin I27 domain folding c...
+超分子 #2: ribosome
+超分子 #3: Tryptophanase operon leader peptide
+超分子 #4: Titin nascent chain
+分子 #1: 50S ribosomal protein L24
+分子 #2: 50S ribosomal protein L32
+分子 #3: 50S ribosomal protein L33
+分子 #4: 50S ribosomal protein L34
+分子 #5: 50S ribosomal protein L35
+分子 #6: 50S ribosomal protein L36
+分子 #7: 50S ribosomal protein L10
+分子 #8: 50S ribosomal protein L7/L12
+分子 #9: Tryptophanase operon leader peptide
+分子 #10: 50S ribosomal protein L25
+分子 #13: 50S ribosomal protein L2
+分子 #14: 50S ribosomal protein L3
+分子 #15: 50S ribosomal protein L4
+分子 #16: 50S ribosomal protein L5
+分子 #17: 50S ribosomal protein L6
+分子 #18: 50S ribosomal protein L9
+分子 #19: 50S ribosomal protein L11
+分子 #20: 50S ribosomal protein L13
+分子 #21: 50S ribosomal protein L14
+分子 #22: 50S ribosomal protein L15
+分子 #23: 50S ribosomal protein L16
+分子 #24: 50S ribosomal protein L17
+分子 #25: 50S ribosomal protein L18
+分子 #26: 50S ribosomal protein L19
+分子 #27: 50S ribosomal protein L20
+分子 #28: 50S ribosomal protein L21
+分子 #29: 50S ribosomal protein L22
+分子 #30: 50S ribosomal protein L23
+分子 #32: 50S ribosomal protein L27
+分子 #33: 50S ribosomal protein L28
+分子 #34: 50S ribosomal protein L29
+分子 #35: 50S ribosomal protein L30
+分子 #36: Titin
+分子 #11: 23S ribosomal RNA
+分子 #12: 5S ribosomal RNA
+分子 #31: Proline tRNA
+分子 #37: MAGNESIUM ION
+分子 #38: ZINC ION
+分子 #39: TRYPTOPHAN
+分子 #40: water
-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: 7.5 |
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グリッド | モデル: Quantifoil R2/2 / 材質: COPPER |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 277.15 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 QUANTUM (4k x 4k) 撮影したグリッド数: 1 / 実像数: 2613 / 平均電子線量: 0.926 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | C2レンズ絞り径: 70.0 µm / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm / 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): 1.0 µm |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER ホルダー冷却材: NITROGEN |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |