+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2j28 | ||||||
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タイトル | MODEL OF E. COLI SRP BOUND TO 70S RNCS | ||||||
要素 |
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キーワード | RIBOSOME / PROTEIN-RNA COMPLEX / SIGNAL RECOGNITION PARTICLE | ||||||
機能・相同性 | 機能・相同性情報 absorption of visible light / G protein-coupled opsin signaling pathway / photoreceptor inner segment membrane / signal recognition particle / 11-cis retinal binding / G protein-coupled photoreceptor activity / signal-recognition-particle GTPase / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane / protein targeting to membrane ...absorption of visible light / G protein-coupled opsin signaling pathway / photoreceptor inner segment membrane / signal recognition particle / 11-cis retinal binding / G protein-coupled photoreceptor activity / signal-recognition-particle GTPase / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane / protein targeting to membrane / negative regulation of cytoplasmic translational initiation / photoreceptor outer segment membrane / stringent response / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / translational termination / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / visual perception / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / response to reactive oxygen species / regulation of cell growth / translational initiation / DNA-templated transcription termination / response to radiation / mRNA 5'-UTR binding / photoreceptor disc membrane / large ribosomal subunit / ribosome binding / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / response to antibiotic / negative regulation of DNA-templated transcription / GTPase activity / mRNA binding / GTP binding / ATP hydrolysis activity / DNA binding / RNA binding / zinc ion binding / membrane / metal ion binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | Escherichia coli (大腸菌) Escherichia coli K-12 (大腸菌) | ||||||
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: 9.5 Å | ||||||
データ登録者 | Halic, M. / Blau, M. / Becker, T. / Mielke, T. / Pool, M.R. / Wild, K. / Sinning, I. / Beckmann, R. | ||||||
引用 | ジャーナル: Nature / 年: 2006 タイトル: Following the signal sequence from ribosomal tunnel exit to signal recognition particle. 著者: Mario Halic / Michael Blau / Thomas Becker / Thorsten Mielke / Martin R Pool / Klemens Wild / Irmgard Sinning / Roland Beckmann / 要旨: Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal ...Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome-nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting. | ||||||
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 | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 2j28.cif.gz | 2.2 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb2j28.ent.gz | 1.7 MB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2j28.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 | 2j28_validation.pdf.gz | 1.3 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 2j28_full_validation.pdf.gz | 2.1 MB | 表示 | |
XML形式データ | 2j28_validation.xml.gz | 259.8 KB | 表示 | |
CIF形式データ | 2j28_validation.cif.gz | 394.9 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/j2/2j28 ftp://data.pdbj.org/pub/pdb/validation_reports/j2/2j28 | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
+50S ribosomal protein ... , 29種, 29分子 01234CDEFGHIJKLMNOPQRSTUVWXYZ
-RNA鎖 , 3種, 3分子 8AB
#7: RNA鎖 | 分子量: 23968.311 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Escherichia coli K-12 (大腸菌) / 株: MRE600 / 発現宿主: Escherichia coli K-12 (大腸菌) |
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#9: RNA鎖 | 分子量: 37848.555 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Escherichia coli K-12 (大腸菌) / 株: MRE600 / 発現宿主: Escherichia coli K-12 (大腸菌) |
#10: RNA鎖 | 分子量: 941612.375 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Escherichia coli K-12 (大腸菌) / 発現宿主: Escherichia coli K-12 (大腸菌) / 参照: GenBank: 1063812051 |
-タンパク質・ペプチド / タンパク質 , 2種, 2分子 79
#6: タンパク質・ペプチド | 分子量: 2121.542 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Escherichia coli K-12 (大腸菌) / 株: MRE600 / 発現宿主: Escherichia coli K-12 (大腸菌) / 参照: UniProt: O62798*PLUS |
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#8: タンパク質 | 分子量: 47362.168 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Escherichia coli (strain K12) (大腸菌) 株: K12 / 遺伝子: FAZ83_22145 / 発現宿主: Escherichia coli K-12 (大腸菌) / 参照: UniProt: A0A6D2WL81, UniProt: P0AGD7*PLUS |
-非ポリマー , 2種, 623分子
#35: 化合物 | ChemComp-MG / #36: 水 | ChemComp-HOH / | |
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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 |
-試料調製
構成要素 | 名称: SRP BOUND TO 70S RNCS / タイプ: RIBOSOME |
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試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | 詳細: CARBON |
急速凍結 | 凍結剤: ETHANE |
-電子顕微鏡撮影
実験機器 | モデル: Tecnai F30 / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TECNAI F30 |
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 | フィルム・検出器のモデル: KODAK SO-163 FILM |
放射波長 | 相対比: 1 |
-解析
EMソフトウェア | 名称: SPIDER / カテゴリ: 3次元再構成 | ||||||||||||
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対称性 | 点対称性: C1 (非対称) | ||||||||||||
3次元再構成 | 解像度: 9.5 Å / 解像度の算出法: FSC 0.5 CUT-OFF / 対称性のタイプ: POINT | ||||||||||||
精密化 | 最高解像度: 9.5 Å | ||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 8 Å
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