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基本情報
登録情報 | ![]() | |||||||||
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タイトル | Chaetomium thermophilum pre-60S State 4 - post-5S rotation with Rix1 complex without Foot - composite structure | |||||||||
![]() | Chaetomium thermophilum pre-60S State 4 - post-5S rotation with Rix1 complex without Foot - composite structure | |||||||||
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機能・相同性 | ![]() : / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() 類似検索 - 分子機能 | |||||||||
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手法 | ![]() ![]() | |||||||||
![]() | Thoms M / Cheng J / Denk T / Berninghausen O / Beckmann R | |||||||||
資金援助 | European Union, 1件
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![]() | ![]() タイトル: Structural insights into coordinating 5S RNP rotation with ITS2 pre-RNA processing during ribosome formation. 著者: Matthias Thoms / Benjamin Lau / Jingdong Cheng / Lisa Fromm / Timo Denk / Nikola Kellner / Dirk Flemming / Paulina Fischer / Laurent Falquet / Otto Berninghausen / Roland Beckmann / Ed Hurt / ![]() ![]() ![]() 要旨: The rixosome defined in Schizosaccharomyces pombe and humans performs diverse roles in pre-ribosomal RNA processing and gene silencing. Here, we isolate and describe the conserved rixosome from ...The rixosome defined in Schizosaccharomyces pombe and humans performs diverse roles in pre-ribosomal RNA processing and gene silencing. Here, we isolate and describe the conserved rixosome from Chaetomium thermophilum, which consists of two sub-modules, the sphere-like Rix1-Ipi3-Ipi1 and the butterfly-like Las1-Grc3 complex, connected by a flexible linker. The Rix1 complex of the rixosome utilizes Sda1 as landing platform on nucleoplasmic pre-60S particles to wedge between the 5S rRNA tip and L1-stalk, thereby facilitating the 180° rotation of the immature 5S RNP towards its mature conformation. Upon rixosome positioning, the other sub-module with Las1 endonuclease and Grc3 polynucleotide-kinase can reach a strategic position at the pre-60S foot to cleave and 5' phosphorylate the nearby ITS2 pre-rRNA. Finally, inward movement of the L1 stalk permits the flexible Nop53 N-terminus with its AIM motif to become positioned at the base of the L1-stalk to facilitate Mtr4 helicase-exosome participation for completing ITS2 removal. Thus, the rixosome structure elucidates the coordination of two central ribosome biogenesis events, but its role in gene silencing may adapt similar strategies. | |||||||||
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マップデータ | ![]() | 17.6 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 89.6 KB 89.6 KB | 表示 表示 | ![]() |
画像 | ![]() | 158.3 KB | ||
Filedesc metadata | ![]() | 20.9 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 8pv8MC ![]() 8ptwC ![]() 8puwC ![]() 8pv1C ![]() 8pv2C ![]() 8pv3C ![]() 8pv4C ![]() 8pv5C ![]() 8pv6C ![]() 8pv7C ![]() 8pvkC ![]() 8pvlC C: 同じ文献を引用 ( M: このマップから作成された原子モデル |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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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 | Chaetomium thermophilum pre-60S State 4 - post-5S rotation with Rix1 complex without Foot - composite structure | ||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.045 Å | ||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
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試料の構成要素
+全体 : Chaetomium thermophilum pre-60S State 2 - pre-5S rotation with Ri...
+超分子 #1: Chaetomium thermophilum pre-60S State 2 - pre-5S rotation with Ri...
+超分子 #2: Ribosome
+超分子 #3: Ribosome assembly protein 4
+分子 #1: 26S rRNA
+分子 #2: 5.8S rRNA
+分子 #54: 5S rRNA
+分子 #3: Large ribosomal subunit protein uL10
+分子 #4: Nucleolar GTP-binding protein 1
+分子 #5: Ribosome biogenesis protein NSA2 homolog
+分子 #6: Putative GTP binding protein
+分子 #7: Eukaryotic translation initiation factor 6
+分子 #8: DUF2423 domain-containing protein
+分子 #9: Ribosome biogenesis protein RLP24
+分子 #10: Zinc finger domain-containing protein
+分子 #11: Nucleolar GTP-binding protein 2
+分子 #12: rRNA-processing protein
+分子 #13: 60S ribosomal protein L2-like protein
+分子 #14: 60S ribosomal protein L3-like protein
+分子 #15: 60S ribosomal protein L4-like protein
+分子 #16: 60S ribosomal protein L6
+分子 #17: 60S ribosomal protein l7-like protein
+分子 #18: 60S ribosomal protein L8
+分子 #19: 60S ribosomal protein l9-like protein
+分子 #20: 60S ribosomal protein L12-like protein
+分子 #21: 60S ribosomal protein L13
+分子 #22: 60S ribosomal protein L14-like protein
+分子 #23: Ribosomal protein L15
+分子 #24: 60S ribosomal protein L16-like protein
+分子 #25: 60S ribosomal protein l17-like protein
+分子 #26: Ribosomal protein L18-like protein
+分子 #27: Ribosomal protein L19
+分子 #28: 60S ribosomal protein L20
+分子 #29: 60S ribosomal protein L22-like protein
+分子 #30: 60S ribosomal protein l23-like protein
+分子 #31: 60S ribosomal protein L25-like protein
+分子 #32: 60S ribosomal protein L26-like protein
+分子 #33: 60S ribosomal protein L27
+分子 #34: 60S ribosomal protein L28-like protein
+分子 #35: 60S ribosomal protein l30-like protein
+分子 #36: Putative 60S ribosomal protein
+分子 #37: 60S ribosomal protein L32-like protein
+分子 #38: 60S ribosomal protein l33-like protein
+分子 #39: Ribosomal protein l34-like protein
+分子 #40: dolichyl-diphosphooligosaccharide--protein glycotransferase
+分子 #41: 60S ribosomal protein L36
+分子 #42: Ribosomal protein L37
+分子 #43: 60S ribosomal protein L38-like protein
+分子 #44: Ribosomal protein eL39
+分子 #45: 60S ribosomal protein L43-like protein
+分子 #46: Pre-rRNA-processing protein IPI3
+分子 #47: Pre-rRNA-processing protein RIX1
+分子 #48: Pre-rRNA-processing protein IPI1
+分子 #49: Protein SDA1
+分子 #50: Ribosomal protein
+分子 #51: Ribosome assembly protein 4
+分子 #52: Putative ribosomal protein
+分子 #53: 60S ribosomal protein l5-like protein
+分子 #55: Putative 60S ribosomal protein
+分子 #56: 60S ribosomal protein l21-like protein
+分子 #57: 60S ribosomal protein L29
+分子 #58: 60S ribosomal protein L41-A
+分子 #59: GUANOSINE-5'-TRIPHOSPHATE
+分子 #60: MAGNESIUM ION
+分子 #61: ZINC ION
+分子 #62: water
-実験情報
-構造解析
手法 | ![]() |
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試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.5 |
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凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: SPOT SCAN / 撮影モード: BRIGHT FIELD![]() |
撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 検出モード: COUNTING / 平均電子線量: 46.0 e/Å2 |
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: NONE |
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初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 2.91 Å / 解像度の算出法: FSC 0.143 CUT-OFF 詳細: Note: This is a composite structure. Values given for consensus refinement. 使用した粒子像数: 21061 |