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データを開く
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基本情報
| 登録情報 | データベース: PDB / ID: 6hma | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| タイトル | Improved model derived from cryo-EM map of Staphylococcus aureus large ribosomal subunit | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
要素 |
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キーワード | RIBOSOME / ribosomal RNA / pathogen / ribosomal protein / cryo-EM | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 機能・相同性 | 機能・相同性情報large ribosomal subunit / transferase activity / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding ...large ribosomal subunit / transferase activity / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / cytoplasm 類似検索 - 分子機能 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 生物種 | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.65 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
データ登録者 | Eyal, Z. / Cimicata, G. / Matzov, D. / Fox, T. / de Val, N. / Zimmerman, E. / Bashan, A. / Yonath, A. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
引用 | ジャーナル: mBio / 年: 2022タイトル: Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis. 著者: Giuseppe Cimicata / Gil Fridkin / Tanaya Bose / Zohar Eyal / Yehuda Halfon / Elinor Breiner-Goldstein / Tara Fox / Ella Zimmerman / Anat Bashan / Natalia de Val / Alexander Wlodawer / Ada Yonath / ![]() 要旨: The ribosome, a multicomponent assembly consisting of RNA and proteins, is a pivotal macromolecular machine that translates the genetic code into proteins. The large ribosomal subunit rRNA helix 68 ...The ribosome, a multicomponent assembly consisting of RNA and proteins, is a pivotal macromolecular machine that translates the genetic code into proteins. The large ribosomal subunit rRNA helix 68 (H68) is a key element in the protein synthesis process, as it coordinates the coupled movements of the actors involved in translocation, including the tRNAs and L1 stalk. Examination of cryo-electron microscopy (cryo-EM) structures of ribosomes incubated for various time durations at physiological temperatures led to the identification of functionally relevant H68 movements. These movements assist the transition of the L1 stalk between its open and closed states. H68 spatial flexibility and its significance to the protein synthesis process were confirmed through its effective targeting with antisense PNA oligomers. Our results suggest that H68 is actively involved in ribosome movements that are central to the elongation process. The mechanism that regulates the translocation step in ribosomes during protein synthesis is not fully understood. In this work, cryo-EM techniques used to image ribosomes from Staphylococcus aureus after incubation at physiological temperature allowed the identification of a conformation of the helix 68 that has never been observed so far. We then propose a mechanism in which such helix, switching between two different conformations, actively coordinates the translocation step, shedding light on the dynamics of ribosomal components. In addition, the relevance of helix 68 to ribosome function and its potential as an antibiotic target was proved by inhibiting Staphylococcus aureus ribosomes activity using oligomers with sequence complementarity. #1: ジャーナル: Proc Natl Acad Sci U S A / 年: 2015タイトル: Structural insights into species-specific features of the ribosome from the pathogen Staphylococcus aureus. 著者: Zohar Eyal / Donna Matzov / Miri Krupkin / Itai Wekselman / Susanne Paukner / Ella Zimmerman / Haim Rozenberg / Anat Bashan / Ada Yonath / ![]() 要旨: The emergence of bacterial multidrug resistance to antibiotics threatens to cause regression to the preantibiotic era. Here we present the crystal structure of the large ribosomal subunit from ...The emergence of bacterial multidrug resistance to antibiotics threatens to cause regression to the preantibiotic era. Here we present the crystal structure of the large ribosomal subunit from Staphylococcus aureus, a versatile Gram-positive aggressive pathogen, and its complexes with the known antibiotics linezolid and telithromycin, as well as with a new, highly potent pleuromutilin derivative, BC-3205. These crystal structures shed light on specific structural motifs of the S. aureus ribosome and the binding modes of the aforementioned antibiotics. Moreover, by analyzing the ribosome structure and comparing it with those of nonpathogenic bacterial models, we identified some unique internal and peripheral structural motifs that may be potential candidates for improving known antibiotics and for use in the design of selective antibiotic drugs against S. aureus. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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 | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 6hma.cif.gz | 1.9 MB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb6hma.ent.gz | 1.5 MB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 6hma.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
| その他 | その他のダウンロード |
-検証レポート
| 文書・要旨 | 6hma_validation.pdf.gz | 1.8 MB | 表示 | wwPDB検証レポート |
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| 文書・詳細版 | 6hma_full_validation.pdf.gz | 1.8 MB | 表示 | |
| XML形式データ | 6hma_validation.xml.gz | 130.9 KB | 表示 | |
| CIF形式データ | 6hma_validation.cif.gz | 225.5 KB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/hm/6hma ftp://data.pdbj.org/pub/pdb/validation_reports/hm/6hma | HTTPS FTP |
-関連構造データ
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リンク
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集合体
| 登録構造単位 | ![]()
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要素
-RNA鎖 , 2種, 2分子 AB
| #1: RNA鎖 | 分子量: 946738.688 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() 参照: GenBank: 1418434134 |
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| #2: RNA鎖 | 分子量: 36974.945 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() 参照: GenBank: 1434110260 |
+50S ribosomal protein ... , 27種, 27分子 CDEFGHIJKLMNOPQRSTUVWXZ1234
-非ポリマー , 1種, 237分子 
| #30: 化合物 | ChemComp-MG / |
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-詳細
| Has protein modification | Y |
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-実験情報
-実験
| 実験 | 手法: 電子顕微鏡法 |
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| EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
| 構成要素 | 名称: Staphylococcus aureus large ribosomal subunit / タイプ: RIBOSOME / Entity ID: #1-#29 / 由来: NATURAL |
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| 由来(天然) | 生物種: ![]() |
| 緩衝液 | pH: 7.6 |
| 試料 | 濃度: 1 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
| 急速凍結 | 凍結剤: ETHANE |
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電子顕微鏡撮影
| 実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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| 顕微鏡 | モデル: FEI TITAN KRIOS |
| 電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
| 電子レンズ | モード: BRIGHT FIELD |
| 撮影 | 電子線照射量: 40 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
| ソフトウェア | 名称: PHENIX / バージョン: 1.13_2998: / 分類: 精密化 |
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| CTF補正 | タイプ: NONE |
| 3次元再構成 | 解像度: 2.65 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 211046 / 対称性のタイプ: POINT |
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