+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 6i0y | ||||||
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タイトル | TnaC-stalled ribosome complex with the titin I27 domain folding close to the ribosomal exit tunnel | ||||||
要素 |
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キーワード | RIBOSOME / Protein folding / ribosomal exit tunnel / nascent chain / titin I27 domain | ||||||
機能・相同性 | 機能・相同性情報 positive regulation of tryptophan metabolic process / transcriptional attenuation by ribosome / sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / tryptophan catabolic process ...positive regulation of tryptophan metabolic process / transcriptional attenuation by ribosome / sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / tryptophan catabolic process / cardiac muscle tissue morphogenesis / protein kinase regulator activity / cardiac muscle hypertrophy / mitotic chromosome condensation / actinin binding / Striated Muscle Contraction / M band / I band / cardiac muscle cell development / structural constituent of muscle / sarcomere organization / stringent response / skeletal muscle thin filament assembly / striated muscle thin filament / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / cardiac muscle contraction / translational termination / striated muscle contraction / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / muscle contraction / protein kinase A signaling / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / condensed nuclear chromosome / response to reactive oxygen species / positive regulation of protein secretion / regulation of cell growth / DNA-templated transcription termination / response to radiation / Z disc / mRNA 5'-UTR binding / response to calcium ion / actin filament binding / large ribosomal subunit / Platelet degranulation / ribosome binding / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / ribosomal large subunit assembly / protein tyrosine kinase activity / cytoplasmic translation / protease binding / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / non-specific serine/threonine protein kinase / calmodulin binding / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / protein serine kinase activity / protein serine/threonine kinase activity / negative regulation of DNA-templated transcription / mRNA binding / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / protein homodimerization activity / DNA binding / RNA binding / extracellular exosome / zinc ion binding / extracellular region / ATP binding / identical protein binding / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | Escherichia coli (大腸菌) Homo sapiens (ヒト) | ||||||
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: 3.2 Å | ||||||
データ登録者 | Su, T. / Kudva, R. / von Heijne, G. / Beckmann, R. | ||||||
資金援助 | スウェーデン, 1件
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引用 | ジャーナル: Proc Natl Acad Sci U S A / 年: 2018 タイトル: Folding pathway of an Ig domain is conserved on and off the ribosome. 著者: Pengfei Tian / Annette Steward / Renuka Kudva / Ting Su / Patrick J Shilling / Adrian A Nickson / Jeffrey J Hollins / Roland Beckmann / Gunnar von Heijne / Jane Clarke / Robert B Best / 要旨: Proteins that fold cotranslationally may do so in a restricted configurational space, due to the volume occupied by the ribosome. How does this environment, coupled with the close proximity of the ...Proteins that fold cotranslationally may do so in a restricted configurational space, due to the volume occupied by the ribosome. How does this environment, coupled with the close proximity of the ribosome, affect the folding pathway of a protein? Previous studies have shown that the cotranslational folding process for many proteins, including small, single domains, is directly affected by the ribosome. Here, we investigate the cotranslational folding of an all-β Ig domain, titin I27. Using an arrest peptide-based assay and structural studies by cryo-EM, we show that I27 folds in the mouth of the ribosome exit tunnel. Simulations that use a kinetic model for the force dependence of escape from arrest accurately predict the fraction of folded protein as a function of length. We used these simulations to probe the folding pathway on and off the ribosome. Our simulations-which also reproduce experiments on mutant forms of I27-show that I27 folds, while still sequestered in the mouth of the ribosome exit tunnel, by essentially the same pathway as free I27, with only subtle shifts of critical contacts from the C to the N terminus. | ||||||
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 | 6i0y.cif.gz | 2.3 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb6i0y.ent.gz | 1.8 MB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 6i0y.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 | 6i0y_validation.pdf.gz | 1.2 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 6i0y_full_validation.pdf.gz | 1.5 MB | 表示 | |
XML形式データ | 6i0y_validation.xml.gz | 176.4 KB | 表示 | |
CIF形式データ | 6i0y_validation.cif.gz | 288.1 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/i0/6i0y ftp://data.pdbj.org/pub/pdb/validation_reports/i0/6i0y | 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 ... , 31種, 31分子 h01234568CDEFGHIJKLMNOPQRSTWXYZ
-RNA鎖 , 3種, 3分子 ABV
#11: RNA鎖 | 分子量: 941306.188 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: GenBank: 1109114233 |
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#12: RNA鎖 | 分子量: 38177.762 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: GenBank: 1430654817 |
#31: RNA鎖 | 分子量: 24876.777 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: GenBank: 1476611766 |
-タンパク質・ペプチド / タンパク質 , 2種, 2分子 7z
#36: タンパク質 | 分子量: 9794.193 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: TTN / 発現宿主: Escherichia coli (大腸菌) / 株 (発現宿主): KC6 参照: UniProt: Q8WZ42, non-specific serine/threonine protein kinase |
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#9: タンパク質・ペプチド | 分子量: 2899.416 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Escherichia coli (大腸菌) / 株: KC6 / 遺伝子: tnaC, tnaL, b3707, JW3685 / 発現宿主: Escherichia coli (大腸菌) / 株 (発現宿主): KC6 / 参照: UniProt: P0AD89 |
-非ポリマー , 4種, 584分子
#37: 化合物 | ChemComp-MG / #38: 化合物 | ChemComp-ZN / | #39: 化合物 | ChemComp-TRP / | #40: 水 | ChemComp-HOH / | |
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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 |
-試料調製
構成要素 |
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由来(天然) |
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由来(組換発現) |
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緩衝液 | pH: 7.5 | ||||||||||||||||||||||||||||||
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||||||||
試料支持 | グリッドの材料: COPPER / グリッドのタイプ: Quantifoil R2/2 | ||||||||||||||||||||||||||||||
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 277.15 K |
-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 / 最大 デフォーカス(公称値): 3000 nm / 最小 デフォーカス(公称値): 1000 nm / Cs: 2.7 mm / C2レンズ絞り径: 70 µm |
試料ホルダ | 凍結剤: NITROGEN 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
撮影 | 電子線照射量: 0.926 e/Å2 フィルム・検出器のモデル: GATAN K2 QUANTUM (4k x 4k) 撮影したグリッド数: 1 / 実像数: 2613 |
画像スキャン | 動画フレーム数/画像: 30 |
-解析
EMソフトウェア |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
粒子像の選択 | 選択した粒子像数: 468015 | ||||||||||||
3次元再構成 | 解像度: 3.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 301510 / 対称性のタイプ: POINT |