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基本情報
登録情報 | データベース: PDB / ID: 5fvm | ||||||
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タイトル | Cryo electron microscopy of a complex of Tor and Lst8 | ||||||
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機能・相同性 | ![]() ![]() ![]() | ||||||
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手法 | ![]() ![]() ![]() | ||||||
![]() | Baretic, D. / Berndt, A. / Ohashi, Y. / Johnson, C.M. / Williams, R.L. | ||||||
![]() | ![]() タイトル: Tor forms a dimer through an N-terminal helical solenoid with a complex topology. 著者: Domagoj Baretić / Alex Berndt / Yohei Ohashi / Christopher M Johnson / Roger L Williams / ![]() 要旨: The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates a range of anabolic and catabolic processes. Tor is present in two complexes, TORC1 and TORC2, in which the Tor-Lst8 ...The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates a range of anabolic and catabolic processes. Tor is present in two complexes, TORC1 and TORC2, in which the Tor-Lst8 heterodimer forms a common sub-complex. We have determined the cryo-electron microscopy (EM) structure of Tor bound to Lst8. Two Tor-Lst8 heterodimers assemble further into a dyad-symmetry dimer mediated by Tor-Tor interactions. The first 1,300 residues of Tor form a HEAT repeat-containing α-solenoid with four distinct segments: a highly curved 800-residue N-terminal 'spiral', followed by a 400-residue low-curvature 'bridge' and an extended 'railing' running along the bridge leading to the 'cap' that links to FAT region. This complex topology was verified by domain insertions and offers a new interpretation of the mTORC1 structure. The spiral of one TOR interacts with the bridge of another, which together form a joint platform for the Regulatory Associated Protein of TOR (RAPTOR) regulatory subunit. | ||||||
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構造の表示
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構造ビューア | 分子: ![]() ![]() |
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-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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非結晶学的対称性 (NCS) | NCS oper: (Code: given / Matrix: (-1),![]() |
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要素
#1: タンパク質 | 分子量: 279407.938 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() #2: タンパク質 | ![]() 分子量: 33952.672 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() 配列の詳細 | THE POLYPEPTIDE HAS AN N-TERMINAL 22 RESIDUE TAG AFTER TEV CLEAVGE. IT WAS CLONED FROM GENOMIC DNA. ...THE POLYPEPTID | |
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-実験情報
-実験
実験 | 手法: ![]() |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: ![]() |
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試料調製
構成要素 | 名称: COMPLEX OF TOR1 WITH LST8 / タイプ: COMPLEX |
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緩衝液 | 名称: 50 MM HEPES PH 7.4 (23 DEG C), 75 MM KCL, 250 MM NACL, 0.3 % (V/V) CHAPS, 1 MM TCEP pH: 7.4 詳細: 50 MM HEPES PH 7.4 (23 DEG C), 75 MM KCL, 250 MM NACL, 0.3 % (V/V) CHAPS, 1 MM TCEP |
試料 | 濃度: 2.5 mg/ml / 包埋: NO / シャドウイング: NO / 染色![]() ![]() |
試料支持 | 詳細: HOLEY CARBON |
急速凍結![]() | 凍結剤: ETHANE 詳細: VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- OTHER, METHOD- 11-13 S AT 4 DEG C, |
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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 / 日付: 2015年5月16日 |
電子銃 | 電子線源![]() ![]() |
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: FEI FALCON II (4k x 4k) |
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解析
EMソフトウェア |
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CTF補正![]() | 詳細: EACH PARTICLE (GCTF) | ||||||||||||
対称性 | 点対称性![]() ![]() | ||||||||||||
3次元再構成![]() | 解像度: 6.7 Å / 粒子像の数: 28877 / ピクセルサイズ(公称値): 1.33 Å / ピクセルサイズ(実測値): 1.33 Å 詳細: THE FAT AND KINASE DOMAINS (FATKIN) WERE FIT USING 4JSV FATKIN AS AN INITIAL MODEL. THE REMAINDER OF THE STRUCTURE WAS FIT WITH A POLY-ALANINE, AND AN APPROXIMATE SEQUENCE REGISTER WAS ...詳細: THE FAT AND KINASE DOMAINS (FATKIN) WERE FIT USING 4JSV FATKIN AS AN INITIAL MODEL. THE REMAINDER OF THE STRUCTURE WAS FIT WITH A POLY-ALANINE, AND AN APPROXIMATE SEQUENCE REGISTER WAS ESTABLISHED BASED ON THE PREDICED HELICAL ELEMENTS IN THE N-TERMINAL REGION AND THE HELICES VISIBLE IN THE EM DENSITY. THE ENTIRE MODEL IS POLY-ALANINE. THE TOPOLOGY OF THE MODEL WAS VERIFIED BY DETERMINING THE STRUCTURES OF VARINTS IN WHICH TENDEM RFPS WERE INSERTED INTO THE STRUCTURE. SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-3329. (DEPOSITION ID: 14248). 対称性のタイプ: POINT | ||||||||||||
原子モデル構築 | プロトコル: FLEXIBLE FIT / 空間: REAL / Target criteria: Cross-correlation coefficient / 詳細: METHOD--FLEXIBLE | ||||||||||||
原子モデル構築 | PDB-ID: 4JSV Accession code: 4JSV / Source name: PDB / タイプ: experimental model | ||||||||||||
精密化 | 最高解像度: 6.7 Å | ||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 6.7 Å
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