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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: 9qlp | ||||||||||||||||||||||||||||||
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| タイトル | NMT1-NAC bound human RNC with full length ARF1 - State 2 | ||||||||||||||||||||||||||||||
要素 |
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キーワード | RIBOSOME / co-translational / N-terminal myristoylation / myristoylation / NMT1 / ARF1 / NAC | ||||||||||||||||||||||||||||||
| 機能・相同性 | 機能・相同性情報negative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development / myristoyltransferase activity / N-terminal peptidyl-glycine N-myristoylation / peptidyl-lysine N6-myristoyltransferase activity / positive regulation of cell proliferation involved in heart morphogenesis / Late Phase of HIV Life Cycle / positive regulation of skeletal muscle tissue growth / mitotic cleavage furrow ingression / translation termination factor activity ...negative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development / myristoyltransferase activity / N-terminal peptidyl-glycine N-myristoylation / peptidyl-lysine N6-myristoyltransferase activity / positive regulation of cell proliferation involved in heart morphogenesis / Late Phase of HIV Life Cycle / positive regulation of skeletal muscle tissue growth / mitotic cleavage furrow ingression / translation termination factor activity / trans-Golgi Network Vesicle Budding / ketone metabolic process / regulation of opsin-mediated signaling pathway / Glycosphingolipid transport / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / translation release factor complex / regulation of receptor internalization / cardiac ventricle development / Intra-Golgi traffic / Activation, myristolyation of BID and translocation to mitochondria / positive regulation of protein localization to mitochondrion / cytoplasmic translational termination / regulation of Arp2/3 complex-mediated actin nucleation / regulation of translational termination / Synthesis of PIPs at the Golgi membrane / glycylpeptide N-tetradecanoyltransferase / glycylpeptide N-tetradecanoyltransferase activity / translation release factor activity / translation release factor activity, codon specific / heart trabecula morphogenesis / skeletal muscle tissue regeneration / protein methylation / translation at presynapse / Nef Mediated CD4 Down-regulation / exit from mitosis / optic nerve development / response to insecticide / sequence-specific mRNA binding / regulation of translation involved in cellular response to UV / eukaryotic 80S initiation complex / negative regulation of formation of translation preinitiation complex / dendritic spine organization / axial mesoderm development / negative regulation of endoplasmic reticulum unfolded protein response / ribosomal protein import into nucleus / regulation of G1 to G0 transition / retinal ganglion cell axon guidance / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / protein-DNA complex disassembly / positive regulation of ubiquitin-protein transferase activity / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / positive regulation of gastrulation / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / long-term synaptic depression / protein tyrosine kinase inhibitor activity / 90S preribosome assembly / protein localization to membrane / peptidyl-tRNA hydrolase activity / IRE1-RACK1-PP2A complex / positive regulation of Golgi to plasma membrane protein transport / nucleolus organization / alpha-beta T cell differentiation / positive regulation of DNA-templated transcription initiation / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / TNFR1-mediated ceramide production / positive regulation of DNA damage response, signal transduction by p53 class mediator / GAIT complex / negative regulation of RNA splicing / TORC2 complex binding / COPI-dependent Golgi-to-ER retrograde traffic / neural crest cell differentiation / supercoiled DNA binding / NF-kappaB complex / negative regulation of DNA repair / G1 to G0 transition / cytoplasmic translational initiation / oxidized purine DNA binding / cysteine-type endopeptidase activator activity involved in apoptotic process / middle ear morphogenesis / 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 / Lysosome Vesicle Biogenesis / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / negative regulation of phagocytosis / Formation of the ternary complex, and subsequently, the 43S complex / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / Golgi Associated Vesicle Biogenesis / protein kinase A binding / Ribosomal scanning and start codon recognition / ion channel inhibitor activity / laminin receptor activity / Synthesis of PIPs at the plasma membrane / Translation initiation complex formation 類似検索 - 分子機能 | ||||||||||||||||||||||||||||||
| 生物種 | 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: 2.75 Å | ||||||||||||||||||||||||||||||
データ登録者 | Denk, T. / Berninghausen, O. / Beckmann, R. | ||||||||||||||||||||||||||||||
| 資金援助 | ドイツ, 1件
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引用 | ジャーナル: Nat Commun / 年: 2026タイトル: Structural basis of co-translational N-myristoylation in humans. 著者: Timo Denk / Paul Monassa / Joanna Musial / Otto Berninghausen / Birgitta Beatrix / Carmela Giglione / Thierry Meinnel / Roland Beckmann / ![]() 要旨: Modifications of proteins occurring during translation are critical for protein localization, stability and function. N-myristoylation is an essential N-terminal lipid modification catalyzed co- ...Modifications of proteins occurring during translation are critical for protein localization, stability and function. N-myristoylation is an essential N-terminal lipid modification catalyzed co-translationally by N-myristoyltransferases (NMTs) which have been identified as promising drug targets. However, its molecular basis in the context of the translating ribosome is not known. Here, we reveal the structural basis for co-translational N-myristoylation by NMT1 on the human ribosome by cryo-electron microscopy (cryo-EM). We show that NMT1 binds near the peptide tunnel exit and interacts with the nascent polypeptide-associated complex (NAC). Unlike other multi-enzyme complexes that act simultaneously, we find that methionine excision by methionine aminopeptidases and N-myristoylation occur sequentially via consecutive binding to the ribosome. Furthermore, our data suggest that NMT1 remains associated with elongating nascent chains, indicating a co-translational chaperone-like function in partnership with NAC. These insights provide a molecular foundation for the understanding of the co-translational N-myristoylation mechanism in humans. #1: ジャーナル: Acta Crystallogr D Struct Biol / 年: 2019 タイトル: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. 著者: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / ...著者: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams / ![]() 要旨: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks. | ||||||||||||||||||||||||||||||
| 履歴 |
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構造の表示
| 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 | 9qlp.cif.gz | 5.5 MB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb9qlp.ent.gz | 表示 | PDB形式 | |
| PDBx/mmJSON形式 | 9qlp.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
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ql/9qlp ftp://data.pdbj.org/pub/pdb/validation_reports/ql/9qlp | HTTPS FTP |
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-関連構造データ
| 関連構造データ | ![]() 53231MC ![]() 9i2dC ![]() 9i2eC ![]() 9qloC ![]() 9qlqC ![]() 9s3bC ![]() 9s3cC ![]() 9s3dC M: このデータのモデリングに利用したマップデータ 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 |
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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 , 6種, 6分子 CMCPL5L7L8S2
| #1: RNA鎖 | 分子量: 306714.188 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) |
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| #2: RNA鎖 | 分子量: 24189.314 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) |
| #5: RNA鎖 | 分子量: 1640222.125 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: GenBank: NR_003287 |
| #6: RNA鎖 | 分子量: 38998.078 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: GenBank: 23898 |
| #7: RNA鎖 | 分子量: 50449.812 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: GenBank: 555853 |
| #55: RNA鎖 | 分子量: 602777.875 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: GenBank: 151415227 |
-タンパク質 , 12種, 12分子 CRCZLILmLsNANBNMSESeSfSg
| #3: タンパク質 | 分子量: 49107.734 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: Naturally occurring K63 hydroxylation / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P62495 |
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| #4: タンパク質 | 分子量: 24539.301 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: ARF1 / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P84077, small monomeric GTPase |
| #16: タンパク質 | 分子量: 24570.949 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q96L21 |
| #45: タンパク質 | 分子量: 14758.394 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P62987 |
| #50: タンパク質 | 分子量: 34309.418 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P05388 |
| #52: タンパク質 | 分子量: 23406.824 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q13765 |
| #53: タンパク質 | 分子量: 17724.037 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P20290 |
| #54: タンパク質 | 分子量: 56884.023 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト)参照: UniProt: P30419, glycylpeptide N-tetradecanoyltransferase, 転移酵素; アシル基を移すもの; アミノアシル基以外のアシル基を移すもの |
| #60: タンパク質 | 分子量: 29654.869 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P62701 |
| #86: タンパク質 | 分子量: 14415.724 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P62861 |
| #87: タンパク質 | 分子量: 18004.041 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P62979 |
| #88: タンパク質 | 分子量: 35115.652 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P63244 |
+60S ribosomal protein ... , 37種, 37分子 LALBLCLDLGLHLJLLLMLNLOLPLQLRLSLTLULVLWLXLYLZLaLbLcLdLeLfLgLh...
-Large ribosomal subunit protein ... , 4種, 4分子 LELFLjLt
| #12: タンパク質 | 分子量: 32810.176 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q02878 |
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| #13: タンパク質 | 分子量: 29290.973 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P18124 |
| #42: タンパク質 | 分子量: 11111.032 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P61927 |
| #51: タンパク質 | 分子量: 17847.619 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P30050 |
+40S ribosomal protein ... , 29種, 29分子 SASBSCSDSFSGSHSISJSKSLSMSNSOSPSQSRSSSTSUSVSWSXSYSZSaSbScSd
-非ポリマー , 4種, 211分子 






| #89: 化合物 | ChemComp-MG / #90: 化合物 | ChemComp-G3D / | #91: 化合物 | ChemComp-ZN / #92: 水 | ChemComp-HOH / | |
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-詳細
| 研究の焦点であるリガンドがあるか | N |
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| Has protein modification | Y |
-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: NMT1-NAC bound human RNC with full length ARF1 - State 2 タイプ: RIBOSOME Entity ID: #1-#3, #5-#47, #49-#51, #55-#88, #52-#53, #4, #54 由来: NATURAL |
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| 由来(天然) | 生物種: Homo sapiens (ヒト) |
| 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 |
| 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: TFS 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): 3500 nm / 最小 デフォーカス(公称値): 500 nm |
| 撮影 | 電子線照射量: 40 e/Å2 フィルム・検出器のモデル: FEI FALCON IV (4k x 4k) |
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解析
| EMソフトウェア | 名称: PHENIX / バージョン: 1.21.2_5419: / カテゴリ: モデル精密化 |
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| CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3次元再構成 | 解像度: 2.75 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 21642 / 対称性のタイプ: POINT |
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万見について




Homo sapiens (ヒト)
ドイツ, 1件
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FIELD EMISSION GUN