+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-12936 | |||||||||
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タイトル | Cryo-EM structure of 70S ribosome stalled with TnaC peptide | |||||||||
マップデータ | ||||||||||
試料 |
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キーワード | Arrest Peptide / Translational stalling / Gene regulation / Translation termination / RIBOSOME | |||||||||
機能・相同性 | 機能・相同性情報 ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / DnaA-L2 complex ...ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / negative regulation of translational initiation / regulation of mRNA stability / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / cytosolic ribosome assembly / response to reactive oxygen species / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / maintenance of translational fidelity / response to radiation / mRNA 5'-UTR binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosome binding / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / molecular adaptor activity / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / metal ion binding / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | Escherichia coli K-12 (大腸菌) / Escherichia coli (strain K12) (大腸菌) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.9 Å | |||||||||
データ登録者 | Su T / Kudva R | |||||||||
引用 | ジャーナル: Nucleic Acids Res / 年: 2021 タイトル: Structural basis of l-tryptophan-dependent inhibition of release factor 2 by the TnaC arrest peptide. 著者: Ting Su / Renuka Kudva / Thomas Becker / Robert Buschauer / Tobias Komar / Otto Berninghausen / Gunnar von Heijne / Jingdong Cheng / Roland Beckmann / 要旨: In Escherichia coli, elevated levels of free l-tryptophan (l-Trp) promote translational arrest of the TnaC peptide by inhibiting its termination. However, the mechanism by which translation- ...In Escherichia coli, elevated levels of free l-tryptophan (l-Trp) promote translational arrest of the TnaC peptide by inhibiting its termination. However, the mechanism by which translation-termination by the UGA-specific decoding release factor 2 (RF2) is inhibited at the UGA stop codon of stalled TnaC-ribosome-nascent chain complexes has so far been ambiguous. This study presents cryo-EM structures for ribosomes stalled by TnaC in the absence and presence of RF2 at average resolutions of 2.9 and 3.5 Å, respectively. Stalled TnaC assumes a distinct conformation composed of two small α-helices that act together with residues in the peptide exit tunnel (PET) to coordinate a single L-Trp molecule. In addition, while the peptidyl-transferase center (PTC) is locked in a conformation that allows RF2 to adopt its canonical position in the ribosome, it prevents the conserved and catalytically essential GGQ motif of RF2 from adopting its active conformation in the PTC. This explains how translation of the TnaC peptide effectively allows the ribosome to function as a L-Trp-specific small-molecule sensor that regulates the tnaCAB operon. | |||||||||
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_12936.map.gz | 110.5 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-12936-v30.xml emd-12936.xml | 66.8 KB 66.8 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_12936.png | 182.6 KB | ||
Filedesc metadata | emd-12936.cif.gz | 13.2 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-12936 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-12936 | 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_12936.map.gz / 形式: CCP4 / 大きさ: 190.1 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: 1.084 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 : 70S ribosome
+超分子 #1: 70S ribosome
+分子 #1: 16S rRNA
+分子 #22: 23S rRNA
+分子 #23: 16S rRNA
+分子 #53: mRNA
+分子 #55: tRNA
+分子 #2: 30S ribosomal protein S2
+分子 #3: 30S ribosomal protein S3
+分子 #4: 30S ribosomal protein S4
+分子 #5: 30S ribosomal protein S5
+分子 #6: 30S ribosomal protein S6, fully modified isoform
+分子 #7: 30S ribosomal protein S7
+分子 #8: 30S ribosomal protein S8
+分子 #9: 30S ribosomal protein S9
+分子 #10: 30S ribosomal protein S10
+分子 #11: 30S ribosomal protein S11
+分子 #12: 30S ribosomal protein S12
+分子 #13: 30S ribosomal protein S13
+分子 #14: 30S ribosomal protein S14
+分子 #15: 30S ribosomal protein S15
+分子 #16: 30S ribosomal protein S16
+分子 #17: 30S ribosomal protein S17
+分子 #18: 30S ribosomal protein S18
+分子 #19: 30S ribosomal protein S19
+分子 #20: 30S ribosomal protein S20
+分子 #21: 30S ribosomal protein S21
+分子 #24: 50S ribosomal protein L2
+分子 #25: 50S ribosomal protein L3
+分子 #26: 50S ribosomal protein L4
+分子 #27: 50S ribosomal protein L5
+分子 #28: 50S ribosomal protein L6
+分子 #29: 50S ribosomal protein L9
+分子 #30: 50S ribosomal protein L13
+分子 #31: 50S ribosomal protein L14
+分子 #32: 50S ribosomal protein L15
+分子 #33: 50S ribosomal protein L16
+分子 #34: 50S ribosomal protein L17
+分子 #35: 50S ribosomal protein L18
+分子 #36: 50S ribosomal protein L19
+分子 #37: 50S ribosomal protein L20
+分子 #38: 50S ribosomal protein L21
+分子 #39: 50S ribosomal protein L22
+分子 #40: 50S ribosomal protein L23
+分子 #41: 50S ribosomal protein L24
+分子 #42: 50S ribosomal protein L25
+分子 #43: 50S ribosomal protein L27
+分子 #44: 50S ribosomal protein L28
+分子 #45: 50S ribosomal protein L29
+分子 #46: 50S ribosomal protein L30
+分子 #47: 50S ribosomal protein L32
+分子 #48: 50S ribosomal protein L33
+分子 #49: 50S ribosomal protein L34
+分子 #50: 50S ribosomal protein L35
+分子 #51: 50S ribosomal protein L36
+分子 #52: 50S ribosomal protein L31
+分子 #54: TnaC
+分子 #56: PAROMOMYCIN
+分子 #57: MAGNESIUM ION
+分子 #58: TRYPTOPHAN
+分子 #59: ZINC ION
-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 |
-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: FEI FALCON II (4k x 4k) 平均電子線量: 28.0 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: OTHER / 詳細: Relion |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 2.9 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 459171 |
初期 角度割当 | タイプ: OTHER / 詳細: Relion |
最終 角度割当 | タイプ: OTHER / 詳細: Relion |