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データを開く
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基本情報
| 登録情報 | ![]() | |||||||||
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| タイトル | Structure of the human 48S initiation complex in open state (h48S AUG open) | |||||||||
マップデータ | ||||||||||
試料 |
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キーワード | 48S / initiation / eIF3 / ternary complex / translation / open state / RIBOSOME | |||||||||
| 機能・相同性 | 機能・相同性情報male germ cell proliferation / translation initiation ternary complex / regulation of translation in response to endoplasmic reticulum stress / glial limiting end-foot / HRI-mediated signaling / response to manganese-induced endoplasmic reticulum stress / Cellular response to mitochondrial stress / viral translational termination-reinitiation / positive regulation of type B pancreatic cell apoptotic process / Response of EIF2AK1 (HRI) to heme deficiency ...male germ cell proliferation / translation initiation ternary complex / regulation of translation in response to endoplasmic reticulum stress / glial limiting end-foot / HRI-mediated signaling / response to manganese-induced endoplasmic reticulum stress / Cellular response to mitochondrial stress / viral translational termination-reinitiation / positive regulation of type B pancreatic cell apoptotic process / Response of EIF2AK1 (HRI) to heme deficiency / Recycling of eIF2:GDP / methionyl-initiator methionine tRNA binding / negative regulation of translational initiation in response to stress / eukaryotic translation initiation factor 3 complex, eIF3e / PERK-mediated unfolded protein response / cap-dependent translational initiation / eukaryotic translation initiation factor 3 complex, eIF3m / PERK regulates gene expression / response to kainic acid / IRES-dependent viral translational initiation / translation reinitiation / eukaryotic translation initiation factor 2 complex / formation of cytoplasmic translation initiation complex / multi-eIF complex / regulation of translational initiation in response to stress / eukaryotic translation initiation factor 3 complex / eukaryotic 43S preinitiation complex / translation factor activity, RNA binding / mRNA cap binding / formation of translation preinitiation complex / eukaryotic 48S preinitiation complex / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / positive regulation of ubiquitin-protein transferase activity / positive regulation of respiratory burst involved in inflammatory response / regulation of translational initiation / positive regulation of gastrulation / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / protein tyrosine kinase inhibitor activity / protein-synthesizing GTPase / IRE1-RACK1-PP2A complex / positive regulation of Golgi to plasma membrane protein transport / nucleolus organization / positive regulation of DNA-templated transcription initiation / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / TNFR1-mediated ceramide production / negative regulation of RNA splicing / neural crest cell differentiation / supercoiled DNA binding / metal-dependent deubiquitinase activity / NF-kappaB complex / negative regulation of DNA repair / cytoplasmic translational initiation / oxidized purine DNA binding / cysteine-type endopeptidase activator activity involved in apoptotic process / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / rRNA modification in the nucleus and cytosol / negative regulation of bicellular tight junction assembly / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / negative regulation of phagocytosis / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / Formation of the ternary complex, and subsequently, the 43S complex / ion channel inhibitor activity / laminin receptor activity / protein kinase A binding / pigmentation / Ribosomal scanning and start codon recognition / positive regulation of mitochondrial depolarization / Translation initiation complex formation / negative regulation of Wnt signaling pathway / fibroblast growth factor binding / monocyte chemotaxis / BH3 domain binding / Protein hydroxylation / negative regulation of translational frameshifting / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / TOR signaling / ribosomal small subunit binding / positive regulation of GTPase activity / SARS-CoV-1 modulates host translation machinery / mTORC1-mediated signalling / iron-sulfur cluster binding / regulation of cell division / Peptide chain elongation / cellular response to ethanol / Selenocysteine synthesis / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / Formation of a pool of free 40S subunits / negative regulation of protein binding / protein serine/threonine kinase inhibitor activity / Eukaryotic Translation Termination / ubiquitin ligase inhibitor activity / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / negative regulation of respiratory burst involved in inflammatory response / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) 類似検索 - 分子機能 | |||||||||
| 生物種 | 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: 4.7 Å | |||||||||
データ登録者 | Yi S-H / Petrychenko V / Schliep JE / Goyal A / Linden A / Chari A / Urlaub H / Stark H / Rodnina MV / Adio S / Fischer N | |||||||||
| 資金援助 | ドイツ, 2件
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引用 | ジャーナル: Nucleic Acids Res / 年: 2022タイトル: Conformational rearrangements upon start codon recognition in human 48S translation initiation complex. 著者: Sung-Hui Yi / Valentyn Petrychenko / Jan Erik Schliep / Akanksha Goyal / Andreas Linden / Ashwin Chari / Henning Urlaub / Holger Stark / Marina V Rodnina / Sarah Adio / Niels Fischer / ![]() 要旨: Selection of the translation start codon is a key step during protein synthesis in human cells. We obtained cryo-EM structures of human 48S initiation complexes and characterized the intermediates of ...Selection of the translation start codon is a key step during protein synthesis in human cells. We obtained cryo-EM structures of human 48S initiation complexes and characterized the intermediates of codon recognition by kinetic methods using eIF1A as a reporter. Both approaches capture two distinct ribosome populations formed on an mRNA with a cognate AUG codon in the presence of eIF1, eIF1A, eIF2-GTP-Met-tRNAiMet and eIF3. The 'open' 40S subunit conformation differs from the human 48S scanning complex and represents an intermediate preceding the codon recognition step. The 'closed' form is similar to reported structures of complexes from yeast and mammals formed upon codon recognition, except for the orientation of eIF1A, which is unique in our structure. Kinetic experiments show how various initiation factors mediate the population distribution of open and closed conformations until 60S subunit docking. Our results provide insights into the timing and structure of human translation initiation intermediates and suggest the differences in the mechanisms of start codon selection between mammals and yeast. | |||||||||
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構造の表示
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ダウンロードとリンク
-EMDBアーカイブ
| マップデータ | emd_14113.map.gz | 162.4 MB | EMDBマップデータ形式 | |
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| ヘッダ (付随情報) | emd-14113-v30.xml emd-14113.xml | 77.4 KB 77.4 KB | 表示 表示 | EMDBヘッダ |
| FSC (解像度算出) | emd_14113_fsc.xml | 12.8 KB | 表示 | FSCデータファイル |
| 画像 | emd_14113.png | 119.2 KB | ||
| マスクデータ | emd_14113_msk_1.map | 178 MB | マスクマップ | |
| Filedesc metadata | emd-14113.cif.gz | 18.3 KB | ||
| その他 | emd_14113_half_map_1.map.gz emd_14113_half_map_2.map.gz | 140.7 MB 140.7 MB | ||
| アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-14113 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-14113 | HTTPS FTP |
-関連構造データ
| 関連構造データ | ![]() 7qp6MC ![]() 7qp7C M: このマップから作成された原子モデル C: 同じ文献を引用 ( |
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| 類似構造データ | 類似検索 - 機能・相同性 F&H 検索 |
| 電子顕微鏡画像生データ | EMPIAR-11005 (タイトル: Conformational rearrangements upon start codon recognition in human 48S translation initiation complexData size: 1.1 TB Data #1: Motion-corrected, dose-weighted micrographs [micrographs - single frame] Data #2: Particles of human 48S IC in open state ("open") [picked particles - single frame - processed] Data #3: Particles of human 48S IC in closed state ("closed") [picked particles - single frame - processed]) |
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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 |
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マップ
| ファイル | ダウンロード / ファイル: emd_14113.map.gz / 形式: CCP4 / 大きさ: 178 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: 1.16 Å | ||||||||||||||||||||||||||||||||||||
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| 対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
| 詳細 | EMDB XML:
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-添付データ
-マスク #1
| ファイル | emd_14113_msk_1.map | ||||||||||||
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| 密度ヒストグラム |
-ハーフマップ: #1
| ファイル | emd_14113_half_map_1.map | ||||||||||||
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| 密度ヒストグラム |
-ハーフマップ: #2
| ファイル | emd_14113_half_map_2.map | ||||||||||||
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| 投影像・断面図 |
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試料の構成要素
+全体 : Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met-mRNA
+超分子 #1: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met-mRNA
+分子 #1: Eukaryotic translation initiation factor 3 subunit B
+分子 #2: Eukaryotic translation initiation factor 3 subunit K
+分子 #3: Eukaryotic translation initiation factor 3 subunit F
+分子 #4: Eukaryotic translation initiation factor 3 subunit L
+分子 #5: Eukaryotic translation initiation factor 3 subunit M
+分子 #7: Eukaryotic translation initiation factor 3 subunit H
+分子 #8: 60S ribosomal protein L41
+分子 #10: 40S ribosomal protein S11
+分子 #11: 40S ribosomal protein S4, X isoform
+分子 #12: 40S ribosomal protein S9
+分子 #13: 40S ribosomal protein S23
+分子 #14: 40S ribosomal protein S30
+分子 #15: 40S ribosomal protein S7
+分子 #16: 40S ribosomal protein S27
+分子 #17: 40S ribosomal protein S13
+分子 #18: 40S ribosomal protein S15a
+分子 #19: 40S ribosomal protein S21
+分子 #20: 40S ribosomal protein S2
+分子 #21: 40S ribosomal protein S17
+分子 #22: 40S ribosomal protein SA
+分子 #23: 40S ribosomal protein S3a
+分子 #24: 40S ribosomal protein S14
+分子 #25: 40S ribosomal protein S26
+分子 #26: 40S ribosomal protein S8
+分子 #27: 40S ribosomal protein S6
+分子 #28: 40S ribosomal protein S24
+分子 #29: 40S ribosomal protein S5
+分子 #30: 40S ribosomal protein S16
+分子 #31: 40S ribosomal protein S3
+分子 #32: 40S ribosomal protein S10
+分子 #33: 40S ribosomal protein S15
+分子 #34: Receptor of activated protein C kinase 1
+分子 #35: 40S ribosomal protein S19
+分子 #36: 40S ribosomal protein S25
+分子 #37: 40S ribosomal protein S18
+分子 #38: 40S ribosomal protein S20
+分子 #39: 40S ribosomal protein S29
+分子 #40: Ubiquitin-40S ribosomal protein S27a
+分子 #41: 40S ribosomal protein S12
+分子 #42: 40S ribosomal protein S28
+分子 #43: Eukaryotic translation initiation factor 3 subunit G
+分子 #44: Eukaryotic translation initiation factor 1
+分子 #45: Eukaryotic translation initiation factor 1A, X-chromosomal
+分子 #46: Eukaryotic translation initiation factor 2 subunit 1
+分子 #47: Eukaryotic translation initiation factor 2 subunit 2
+分子 #48: Eukaryotic translation initiation factor 2 subunit 3
+分子 #49: Eukaryotic translation initiation factor 3 subunit A
+分子 #50: Eukaryotic translation initiation factor 3 subunit E
+分子 #52: Eukaryotic translation initiation factor 3 subunit D
+分子 #53: Eukaryotic translation initiation factor 3 subunit C
+分子 #6: mRNA
+分子 #9: 18S rRNA
+分子 #51: Initiator Met-tRNA-i
+分子 #54: ZINC ION
+分子 #55: 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 |
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試料調製
| 緩衝液 | pH: 7.5 詳細: 20 mM Hepes, pH 7.5, 95 mM KOAc, 3.75 mM Mg(OAc)2, 1 mM ATP, 0.5 mM GTP, 0.25 mM spermidine, 2 mM DTT, 0.4 U/uL RiboLock RNase inhibitor |
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| グリッド | モデル: Quantifoil R3.5/1 / 材質: COPPER / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: CONTINUOUS |
| 凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 277 K / 装置: FEI VITROBOT MARK IV 詳細: Cryo-EM grids were prepared by floating home-made continuous carbon on 40 ul sample in the wells of teflon block (custom-made). The sample-covered carbon was then adsorbed to an EM grid.. |
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電子顕微鏡法
| 顕微鏡 | FEI TITAN KRIOS |
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| 詳細 | Aberration corrections performed using Cs image corrector (CEOS company) |
| 撮影 | フィルム・検出器のモデル: FEI FALCON III (4k x 4k) 検出モード: INTEGRATING / デジタル化 - サイズ - 横: 4096 pixel / デジタル化 - サイズ - 縦: 4096 pixel / 撮影したグリッド数: 1 / 実像数: 15544 / 平均露光時間: 1.0 sec. / 平均電子線量: 48.0 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 / Cs: 0.01 mm / 最大 デフォーカス(公称値): 4.0 µm / 最小 デフォーカス(公称値): 1.5 µm / 倍率(公称値): 59000 |
| 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 |
ムービー
コントローラー
万見について




キーワード
Homo sapiens (ヒト)
データ登録者
ドイツ, 2件
引用







































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Y (Row.)
Z (Col.)













































解析
FIELD EMISSION GUN



