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データを開く
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基本情報
登録情報 | ![]() | |||||||||||||||
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タイトル | H. sapiens MCM bound to double stranded DNA and ORC6 as part of the MCM-ORC complex | |||||||||||||||
![]() | Consensus map of the human ORC bound to the amino-terminal side of a DNA-loaded MCM hexamer. The complex is referred to as MO*. | |||||||||||||||
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![]() | AAA+ ATPase / DNA helicase / REPLICATION | |||||||||||||||
機能・相同性 | ![]() CDC6 association with the ORC:origin complex / origin recognition complex / E2F-enabled inhibition of pre-replication complex formation / Switching of origins to a post-replicative state / Unwinding of DNA / nuclear origin of replication recognition complex / Regulation of MITF-M-dependent genes involved in DNA replication, damage repair and senescence / alpha DNA polymerase:primase complex / mitotic DNA replication / regulation of phosphorylation ...CDC6 association with the ORC:origin complex / origin recognition complex / E2F-enabled inhibition of pre-replication complex formation / Switching of origins to a post-replicative state / Unwinding of DNA / nuclear origin of replication recognition complex / Regulation of MITF-M-dependent genes involved in DNA replication, damage repair and senescence / alpha DNA polymerase:primase complex / mitotic DNA replication / regulation of phosphorylation / CMG complex / MCM complex / double-strand break repair via break-induced replication / mitotic DNA replication initiation / regulation of DNA-templated DNA replication initiation / DNA strand elongation involved in DNA replication / cochlea development / DNA replication origin binding / Activation of the pre-replicative complex / DNA replication initiation / Activation of ATR in response to replication stress / DNA helicase activity / Assembly of the ORC complex at the origin of replication / cellular response to interleukin-4 / cellular response to epidermal growth factor stimulus / Assembly of the pre-replicative complex / helicase activity / fibrillar center / Orc1 removal from chromatin / cellular response to xenobiotic stimulus / nucleosome assembly / single-stranded DNA binding / DNA helicase / histone binding / chromosome, telomeric region / DNA replication / cell population proliferation / cilium / intracellular membrane-bounded organelle / apoptotic process / DNA damage response / chromatin / perinuclear region of cytoplasm / enzyme binding / ATP hydrolysis activity / DNA binding / zinc ion binding / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||||||||
生物種 | ![]() | |||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.6 Å | |||||||||||||||
![]() | Greiwe JF / Weissmann F / Diffley JFX / Costa A | |||||||||||||||
資金援助 | ![]()
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![]() | 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. #1: ![]() タイトル: MCM Double Hexamer Loading Visualised with Human Proteins 著者: Weissmann F / Greiwe JF / Puhringer T / Miller TCR / Diffley JFX / Costa A | |||||||||||||||
履歴 |
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構造の表示
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ダウンロードとリンク
-EMDBアーカイブ
マップデータ | ![]() | 230.2 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 41.5 KB 41.5 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 13.3 KB | 表示 | ![]() |
画像 | ![]() | 113.7 KB | ||
マスクデータ | ![]() | 244.1 MB | ![]() | |
Filedesc metadata | ![]() | 11.5 KB | ||
その他 | ![]() ![]() ![]() | 230.3 MB 226.9 MB 226.9 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 985.9 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 985.5 KB | 表示 | |
XML形式データ | ![]() | 22 KB | 表示 | |
CIF形式データ | ![]() | 28.6 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 8s0bMC ![]() 8s09C ![]() 8s0aC ![]() 8s0cC ![]() 8s0dC ![]() 8s0eC ![]() 8s0fC C: 同じ文献を引用 ( M: このマップから作成された原子モデル |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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リンク
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||
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注釈 | Consensus map of the human ORC bound to the amino-terminal side of a DNA-loaded MCM hexamer. The complex is referred to as MO*. | ||||||||||||||||||||||||||||||||||||
投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.08 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-マスク #1
ファイル | ![]() | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-追加マップ: Local refinement of the MCM2-7 in the MCM-ORC complex.
ファイル | emd_19620_additional_1.map | ||||||||||||
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注釈 | Local refinement of the MCM2-7 in the MCM-ORC complex. | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: Half map 2 of the main map
ファイル | emd_19620_half_map_1.map | ||||||||||||
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注釈 | Half map 2 of the main map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: Half map 1 of the main map
ファイル | emd_19620_half_map_2.map | ||||||||||||
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注釈 | Half map 1 of the main map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
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試料の構成要素
+全体 : H. sapiens MCM bound to double stranded DNA and ORC6 as part of t...
+超分子 #1: H. sapiens MCM bound to double stranded DNA and ORC6 as part of t...
+超分子 #2: H. sapiens ORC6
+超分子 #3: Double stranded DNA
+超分子 #4: H. sapiens MCM2-7
+分子 #1: Origin recognition complex subunit 6
+分子 #2: DNA replication licensing factor MCM2
+分子 #3: DNA replication licensing factor MCM3
+分子 #4: DNA replication licensing factor MCM4
+分子 #5: DNA replication licensing factor MCM5
+分子 #6: DNA replication licensing factor MCM6
+分子 #7: DNA replication licensing factor MCM7
+分子 #8: DNA (45-mer)
+分子 #9: DNA (45-mer)
+分子 #10: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
+分子 #11: MAGNESIUM ION
+分子 #12: ZINC ION
+分子 #13: ADENOSINE-5'-DIPHOSPHATE
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.5 |
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グリッド | モデル: UltrAuFoil R1.2/1.3 / 材質: GOLD / メッシュ: 300 / 支持フィルム - 材質: GRAPHENE OXIDE |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 90 % / チャンバー内温度: 295 K / 装置: FEI VITROBOT MARK IV |
詳細 | The MCM recruitment reaction was reconstituted in vitro using purified H. sapiens proteins, a short DNA template and ATPgammaS. Four microlitres of the entire reaction was applied on a grid and incubated for 1 min at room temperature before blotting with filter paper for 5 s and plunge-freezing in liquid ethane. |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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特殊光学系 | エネルギーフィルター - 名称: GIF Bioquantum |
撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 検出モード: COUNTING / 撮影したグリッド数: 1 / 実像数: 31569 / 平均露光時間: 9.4 sec. / 平均電子線量: 49.28 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2.5 µm / 最小 デフォーカス(公称値): 1.0 µm / 倍率(公称値): 130000 |
試料ステージ | ホルダー冷却材: NITROGEN |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
-原子モデル構築 1
初期モデル |
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得られたモデル | ![]() PDB-8s0b: |