+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-10705 | |||||||||
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タイトル | Cryo-EM structure of an Escherichia coli 70S ribosome in complex with antibiotic TetracenomycinX | |||||||||
マップデータ | ||||||||||
試料 |
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キーワード | tetracenomycin / RIBOSOME | |||||||||
機能・相同性 | 機能・相同性情報 dormancy process / negative regulation of translational elongation / negative regulation of cytoplasmic translational initiation / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / ribosomal small subunit binding / RNA folding / transcriptional attenuation ...dormancy process / negative regulation of translational elongation / negative regulation of cytoplasmic translational initiation / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / ribosomal small subunit binding / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / four-way junction DNA binding / 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 / transcription elongation factor complex / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / DNA endonuclease activity / response to reactive oxygen species / transcription antitermination / regulation of cell growth / translational initiation / 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 biogenesis / 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 / 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: 2.86 Å | |||||||||
データ登録者 | Wieland M / Wilson DN | |||||||||
資金援助 | ドイツ, 1件
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引用 | ジャーナル: Nat Chem Biol / 年: 2020 タイトル: Tetracenomycin X inhibits translation by binding within the ribosomal exit tunnel. 著者: Ilya A Osterman / Maximiliane Wieland / Tinashe P Maviza / Kseniya A Lashkevich / Dmitrii A Lukianov / Ekaterina S Komarova / Yuliya V Zakalyukina / Robert Buschauer / Dmitrii I Shiriaev / ...著者: Ilya A Osterman / Maximiliane Wieland / Tinashe P Maviza / Kseniya A Lashkevich / Dmitrii A Lukianov / Ekaterina S Komarova / Yuliya V Zakalyukina / Robert Buschauer / Dmitrii I Shiriaev / Semen A Leyn / Jaime E Zlamal / Mikhail V Biryukov / Dmitry A Skvortsov / Vadim N Tashlitsky / Vladimir I Polshakov / Jingdong Cheng / Yury S Polikanov / Alexey A Bogdanov / Andrei L Osterman / Sergey E Dmitriev / Roland Beckmann / Olga A Dontsova / Daniel N Wilson / Petr V Sergiev / 要旨: The increase in multi-drug resistant pathogenic bacteria is making our current arsenal of clinically used antibiotics obsolete, highlighting the urgent need for new lead compounds with distinct ...The increase in multi-drug resistant pathogenic bacteria is making our current arsenal of clinically used antibiotics obsolete, highlighting the urgent need for new lead compounds with distinct target binding sites to avoid cross-resistance. Here we report that the aromatic polyketide antibiotic tetracenomycin (TcmX) is a potent inhibitor of protein synthesis, and does not induce DNA damage as previously thought. Despite the structural similarity to the well-known translation inhibitor tetracycline, we show that TcmX does not interact with the small ribosomal subunit, but rather binds to the large subunit, within the polypeptide exit tunnel. This previously unappreciated binding site is located adjacent to the macrolide-binding site, where TcmX stacks on the noncanonical basepair formed by U1782 and U2586 of the 23S ribosomal RNA. Although the binding site is distinct from the macrolide antibiotics, our results indicate that like macrolides, TcmX allows translation of short oligopeptides before further translation is blocked. | |||||||||
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_10705.map.gz | 16 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-10705-v30.xml emd-10705.xml | 72.6 KB 72.6 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_10705_fsc.xml | 12.7 KB | 表示 | FSCデータファイル |
画像 | emd_10705.png | 205.1 KB | ||
Filedesc metadata | emd-10705.cif.gz | 13.3 KB | ||
その他 | emd_10705_additional.map.gz emd_10705_half_map_1.map.gz emd_10705_half_map_2.map.gz | 18.4 MB 140.4 MB 140.4 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-10705 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-10705 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_10705_validation.pdf.gz | 842.8 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_10705_full_validation.pdf.gz | 842.4 KB | 表示 | |
XML形式データ | emd_10705_validation.xml.gz | 21.1 KB | 表示 | |
CIF形式データ | emd_10705_validation.cif.gz | 26.8 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-10705 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-10705 | 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_10705.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
-追加マップ: #1
ファイル | emd_10705_additional.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #1
ファイル | emd_10705_half_map_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #2
ファイル | emd_10705_half_map_2.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-試料の構成要素
+全体 : Cryo-EM structure of the antibiotic TetracenomycinX bound to the ...
+超分子 #1: Cryo-EM structure of the antibiotic TetracenomycinX bound to the ...
+分子 #1: 16S ribosomal RNA
+分子 #22: 23S ribosomal RNA
+分子 #23: 5S ribosomal RNA
+分子 #53: E-site 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
+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: Ribosome hibernation promoting factor
+分子 #55: Tetracenomycin X
+分子 #56: MAGNESIUM 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: 7.5 |
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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: SPOT SCAN / 撮影モード: BRIGHT FIELD |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |