+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 4uer | ||||||||||||
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タイトル | 40S-eIF1-eIF1A-eIF3-eIF3j translation initiation complex from Lachancea kluyveri | ||||||||||||
要素 |
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キーワード | TRANSLATION (翻訳 (生物学)) / EIF3 (EIF3) / TRANSLATION INITIATION | ||||||||||||
機能・相同性 | 機能・相同性情報 eukaryotic translation initiation factor 3 complex / eukaryotic 43S preinitiation complex / formation of cytoplasmic translation initiation complex / eukaryotic 48S preinitiation complex / translation initiation factor binding / translation initiation factor activity / rRNA processing / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit ...eukaryotic translation initiation factor 3 complex / eukaryotic 43S preinitiation complex / formation of cytoplasmic translation initiation complex / eukaryotic 48S preinitiation complex / translation initiation factor binding / translation initiation factor activity / rRNA processing / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / rRNA binding / リボソーム / structural constituent of ribosome / ribonucleoprotein complex / 翻訳 (生物学) / RNA binding / zinc ion binding / metal ion binding / 細胞質基質 / 細胞質 類似検索 - 分子機能 | ||||||||||||
生物種 | LACHANCEA KLUYVERI (菌類) | ||||||||||||
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: 6.47 Å | ||||||||||||
データ登録者 | Aylett, C.H.S. / Boehringer, D. / Erzberger, J.P. / Schaefer, T. / Ban, N. | ||||||||||||
引用 | ジャーナル: Nat Struct Mol Biol / 年: 2015 タイトル: Structure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complex. 著者: Christopher H S Aylett / Daniel Boehringer / Jan P Erzberger / Tanja Schaefer / Nenad Ban / 要旨: Eukaryotic translation initiation requires cooperative assembly of a large protein complex at the 40S ribosomal subunit. We have resolved a budding yeast initiation complex by cryo-EM, allowing ...Eukaryotic translation initiation requires cooperative assembly of a large protein complex at the 40S ribosomal subunit. We have resolved a budding yeast initiation complex by cryo-EM, allowing placement of prior structures of eIF1, eIF1A, eIF3a, eIF3b and eIF3c. Our structure highlights differences in initiation-complex binding to the ribosome compared to that of mammalian eIF3, demonstrates a direct contact between eIF3j and eIF1A and reveals the network of interactions between eIF3 subunits. | ||||||||||||
履歴 |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "0A" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "0A" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "LA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "QA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-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 | 4uer.cif.gz | 2.2 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb4uer.ent.gz | 1.7 MB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 4uer.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/ue/4uer ftp://data.pdbj.org/pub/pdb/validation_reports/ue/4uer | HTTPS FTP |
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-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
+タンパク質 , 38種, 38分子 0123456789BCDEFGHIJKLMNOPQRSTU...
-RNA鎖 / 非ポリマー , 2種, 5分子 A
#11: RNA鎖 | 分子量: 571936.750 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) LACHANCEA KLUYVERI (菌類) |
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#40: 化合物 | ChemComp-ZN / |
-詳細
配列の詳細 | THE 40S SUBUNIT IS TAKEN FROM PDBS 3U5B,3U5G AND RECHAINED TO MATCH 2XZM THE UNIPROT SC EIF3B ...THE 40S SUBUNIT IS TAKEN FROM PDBS 3U5B,3U5G AND RECHAINED TO MATCH 2XZM THE UNIPROT SC EIF3B SEQUENCE USES AN UPSTREAM START CODON THOUGHT TO BE DISFAVOURE |
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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: LACHANCEA KLUYVERI 40S- EIF1- EIF1A-EIF3-EIF3J INITIATION COMPLEX タイプ: RIBOSOME / 詳細: MICROGRAPHS SELECTED BY CTF |
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緩衝液 | 名称: 25 MM K-HEPES, 10 MM MGCL2, 75 MM KCL, 0.5 MM TCEP / pH: 7.6 / 詳細: 25 MM K-HEPES, 10 MM MGCL2, 75 MM KCL, 0.5 MM TCEP |
試料 | 濃度: 0.2 mg/ml / 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 | 装置: HOMEMADE PLUNGER / 凍結剤: ETHANE 詳細: VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 75, TEMPERATURE- 120, INSTRUMENT- HOMEMADE PLUNGER, METHOD- 5 SECONDS BLOTTING BEFORE PLUNGING., DETAILS- CARBON FLOATED ON THE SAMPLE PRIOR TO ...詳細: VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 75, TEMPERATURE- 120, INSTRUMENT- HOMEMADE PLUNGER, METHOD- 5 SECONDS BLOTTING BEFORE PLUNGING., DETAILS- CARBON FLOATED ON THE SAMPLE PRIOR TO RECOVERY ONTO THE GRID AND FLASH -FREEZING. |
-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 / 日付: 2014年4月6日 |
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 FIELDBright-field microscopy / 倍率(公称値): 59000 X / 倍率(補正後): 100719 X / 最大 デフォーカス(公称値): 5000 nm / 最小 デフォーカス(公称値): 1000 nm / Cs: 2.7 mm |
試料ホルダ | 温度: 100 K |
撮影 | 電子線照射量: 25 e/Å2 フィルム・検出器のモデル: FEI FALCON II (4k x 4k) |
放射波長 | 相対比: 1 |
-解析
EMソフトウェア |
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CTF補正 | 詳細: BY IMAGE | ||||||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||||||
3次元再構成 | 手法: MAXIMUM A POSTERIORI PROJECTION MATCHING / 解像度: 6.47 Å / 粒子像の数: 27354 / ピクセルサイズ(公称値): 1.39 Å / ピクセルサイズ(実測値): 1.39 Å 詳細: THIS DEPOSITION DETAILS AN S. CEREVISIAE MODEL FOR THE CLOSELY RELATED L. KLUYVERI STRUCTURE. INITIAL PLACEMENT OF FOLDED DOMAINS WAS ACCORDING TO THE MASS-SPECTROMETRY MODEL IN DOMAINS WERE ...詳細: THIS DEPOSITION DETAILS AN S. CEREVISIAE MODEL FOR THE CLOSELY RELATED L. KLUYVERI STRUCTURE. INITIAL PLACEMENT OF FOLDED DOMAINS WAS ACCORDING TO THE MASS-SPECTROMETRY MODEL IN DOMAINS WERE FITTED INTO CRYOEM DENSITY LOW-PASS FILTERED AT MEAN LOCAL RESOLUTION AS RIGID BODIES USING CALCULATED DENSITIES GENERATED AT THE SAME RESOLUTION. CORRELATION COEFFICIENT WAS USED AS THE TARGET FUNCTION IN CHIMERA. THE RRM DOMAIN OF EIF3B IS DEPOSITED AS CA TRACE ONLY TO INDICATE THAT ITS POSITION HAS LOWER ANGULAR CONFIDENCE BECAUSE THE DOMAIN IS EXTREMELY SMALL AND GENERATED NO DIRECT CROSS-LINKS TO THE 40S TO AID PLACEMENT. EIF3B HAS BEEN NUMBERED ACCORDING TO THE SECOND START CODON AS THIS IS THOUGHT TO BE THE PREDOMINANT FORM OF THE PROTEIN IN VIVO. SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2845. 対称性のタイプ: POINT | ||||||||||||||||
原子モデル構築 | プロトコル: RIGID BODY FIT / 空間: REAL / Target criteria: Cross-correlation coefficient / 詳細: METHOD--RIGID BODY | ||||||||||||||||
原子モデル構築 | PDB-ID: 3U5B 3u5b Accession code: 3U5B / Source name: PDB / タイプ: experimental model | ||||||||||||||||
精密化 | 最高解像度: 6.47 Å | ||||||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 6.47 Å
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