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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: EMDB / ID: EMD-6400 | |||||||||
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| タイトル | Electron microscopy of BRCA1(5832insC) mutant-RNAP II transcriptional complex | |||||||||
マップデータ | Reconstruction of BRCA1-RNAP II mutant complex | |||||||||
試料 |
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キーワード | transcription / DNA damage repair / breast cancer / protein | |||||||||
| 機能・相同性 | 機能・相同性情報negative regulation of mRNA 3'-end processing / histone H2AK127 ubiquitin ligase activity / histone H2AK129 ubiquitin ligase activity / Defective DNA double strand break response due to BRCA1 loss of function / Defective DNA double strand break response due to BARD1 loss of function / BRCA1-BARD1 complex / BRCA1-B complex / BRCA1-A complex / BRCA1-C complex / microfibril binding ...negative regulation of mRNA 3'-end processing / histone H2AK127 ubiquitin ligase activity / histone H2AK129 ubiquitin ligase activity / Defective DNA double strand break response due to BRCA1 loss of function / Defective DNA double strand break response due to BARD1 loss of function / BRCA1-BARD1 complex / BRCA1-B complex / BRCA1-A complex / BRCA1-C complex / microfibril binding / negative regulation of centriole replication / sex-chromosome dosage compensation / random inactivation of X chromosome / ubiquitin-modified histone reader activity / chordate embryonic development / cellular response to indole-3-methanol / gamma-tubulin ring complex / negative regulation of intracellular estrogen receptor signaling pathway / nuclear ubiquitin ligase complex / DNA strand resection involved in replication fork processing / negative regulation of fatty acid biosynthetic process / homologous recombination / Regulation of MITF-M-dependent genes involved in DNA replication, damage repair and senescence / tissue homeostasis / protein K6-linked ubiquitination / regulation of phosphorylation / lateral element / Impaired BRCA2 binding to PALB2 / regulation of DNA damage checkpoint / XY body / mitotic G2/M transition checkpoint / negative regulation of protein export from nucleus / RNA polymerase binding / DNA repair complex / DNA damage tolerance / centrosome cycle / Abortive elongation of HIV-1 transcript in the absence of Tat / FGFR2 alternative splicing / MicroRNA (miRNA) biogenesis / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Viral Messenger RNA Synthesis / Resolution of D-loop Structures through Holliday Junction Intermediates / Signaling by FGFR2 IIIa TM / intracellular membraneless organelle / HDR through Single Strand Annealing (SSA) / response to ionizing radiation / negative regulation of gene expression via chromosomal CpG island methylation / Impaired BRCA2 binding to RAD51 / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / Transcriptional Regulation by E2F6 / mitotic G2 DNA damage checkpoint signaling / mRNA Splicing - Minor Pathway / PIWI-interacting RNA (piRNA) biogenesis / negative regulation of cell cycle / Processing of Capped Intron-Containing Pre-mRNA / negative regulation of reactive oxygen species metabolic process / Presynaptic phase of homologous DNA pairing and strand exchange / positive regulation of vascular endothelial growth factor production / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / ubiquitin ligase complex / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / SUMOylation of DNA damage response and repair proteins / regulation of DNA repair / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / protein autoubiquitination / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / RNA Polymerase II Pre-transcription Events / FLT3 signaling by CBL mutants / IRAK2 mediated activation of TAK1 complex / Prevention of phagosomal-lysosomal fusion / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex 類似検索 - 分子機能 | |||||||||
| 生物種 | Homo sapiens (ヒト) | |||||||||
| 手法 | 単粒子再構成法 / ネガティブ染色法 / 解像度: 26.0 Å | |||||||||
データ登録者 | Winton CE / Gilmore BL / Demmert AC / Tanner JR / Bowman S / Karageorge V / Patel K / Sheng Z / Kelly DF | |||||||||
引用 | ジャーナル: Nat Struct Biol / 年: 2001タイトル: Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1. 著者: R S Williams / R Green / J N Glover / ![]() 要旨: The C-terminal BRCT region of BRCA1 is essential for its DNA repair, transcriptional regulation and tumor suppressor functions. Here we determine the crystal structure of the BRCT domain of human ...The C-terminal BRCT region of BRCA1 is essential for its DNA repair, transcriptional regulation and tumor suppressor functions. Here we determine the crystal structure of the BRCT domain of human BRCA1 at 2.5 A resolution. The domain contains two BRCT repeats that adopt similar structures and are packed together in a head-to-tail arrangement. Cancer-causing missense mutations occur at the interface between the two repeats and destabilize the structure. The manner by which the two BRCT repeats interact in BRCA1 may represent a general mode of interaction between homologous domains within proteins that interact to regulate the cellular response to DNA damage. The structure provides a basis to predict the structural consequences of uncharacterized BRCA1 mutations. #3: ジャーナル: NAT.STRUCT.BIOL. / 年: 2001タイトル: Structure of a BRCA1-BARD1 heterodimeric RING-RING complex 著者: Brzovic PS / Rajagopal P / Hoyt DW / King MC / Klevit RE #4: ジャーナル: J.MOL.BIOL. / 年: 1987タイトル: Structure of ubiquitin refined at 1.8 A resolution 著者: Vijay-Kumar S / Bugg CE / Cook WJ | |||||||||
| 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 | EMマップ: SurfView Molmil Jmol/JSmol |
| 添付画像 |
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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 | emd_6400.map.gz | 6.2 MB | EMDBマップデータ形式 | |
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| ヘッダ (付随情報) | emd-6400-v30.xml emd-6400.xml | 21.7 KB 21.7 KB | 表示 表示 | EMDBヘッダ |
| 画像 | 400_6400.gif 80_6400.gif | 61.5 KB 14.3 KB | ||
| アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-6400 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6400 | HTTPS FTP |
-検証レポート
| 文書・要旨 | emd_6400_validation.pdf.gz | 78.8 KB | 表示 | EMDB検証レポート |
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| 文書・詳細版 | emd_6400_full_validation.pdf.gz | 77.9 KB | 表示 | |
| XML形式データ | emd_6400_validation.xml.gz | 494 B | 表示 | |
| アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6400 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6400 | HTTPS FTP |
-関連構造データ
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リンク
| EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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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 | ダウンロード / ファイル: emd_6400.map.gz / 形式: CCP4 / 大きさ: 12.6 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| 注釈 | Reconstruction of BRCA1-RNAP II mutant complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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: 4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 密度 |
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| 対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
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試料の構成要素
-全体 : Mutant BRCA1(5382insC)-RNAP II transcriptional assemblies isolate...
| 全体 | 名称: Mutant BRCA1(5382insC)-RNAP II transcriptional assemblies isolated from hereditary breast cancer cells |
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| 要素 |
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-超分子 #1000: Mutant BRCA1(5382insC)-RNAP II transcriptional assemblies isolate...
| 超分子 | 名称: Mutant BRCA1(5382insC)-RNAP II transcriptional assemblies isolated from hereditary breast cancer cells タイプ: sample / ID: 1000 集合状態: one mutant BRCA1(5382insC) molecule binds to one polymerase complex Number unique components: 4 |
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| 分子量 | 理論値: 800 KDa |
-分子 #1: RNA Polyermase II core
| 分子 | 名称: RNA Polyermase II core / タイプ: protein_or_peptide / ID: 1 / Name.synonym: Pol2 / コピー数: 1 / 組換発現: No / データベース: NCBI |
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| 由来(天然) | 生物種: Homo sapiens (ヒト) / 別称: human / 組織: breast / 細胞: tumor / Organelle: nucleus |
| 分子量 | 理論値: 500 KDa |
| 配列 | UniProtKB: DNA-directed RNA polymerase II subunit RPB1 |
-分子 #2: BRCA1
| 分子 | 名称: BRCA1 / タイプ: protein_or_peptide / ID: 2 詳細: Mutated BRCA1 was attached to tunable microchips using antibodies against the BRCA1 C-terminal domain. コピー数: 1 / 集合状態: monomer / 組換発現: No / データベース: NCBI |
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| 由来(天然) | 生物種: Homo sapiens (ヒト) / 別称: human / 組織: breast / 細胞: tumor / Organelle: nucleus |
| 分子量 | 理論値: 200 KDa |
| 配列 | UniProtKB: Breast cancer type 1 susceptibility protein |
-分子 #3: BARD1
| 分子 | 名称: BARD1 / タイプ: protein_or_peptide / ID: 3 / コピー数: 1 / 集合状態: monomer / 組換発現: No / データベース: NCBI |
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| 由来(天然) | 生物種: Homo sapiens (ヒト) / 別称: human / 組織: breast / 細胞: tumor / Organelle: nucleus |
| 分子量 | 理論値: 87 KDa |
| 配列 | UniProtKB: BRCA1-associated RING domain protein 1 |
-分子 #4: Ubiquitin
| 分子 | 名称: Ubiquitin / タイプ: protein_or_peptide / ID: 4 / コピー数: 2 / 集合状態: monomer / 組換発現: No / データベース: NCBI |
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| 由来(天然) | 生物種: Homo sapiens (ヒト) / 別称: human / 組織: breast / 細胞: tumor / Organelle: nucleus |
| 分子量 | 理論値: 8 KDa |
| 配列 | UniProtKB: Polyubiquitin-C |
-実験情報
-構造解析
| 手法 | ネガティブ染色法 |
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解析 | 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 / 詳細: 50 mM HEPES, 150 mM NaCl, 10 mM MgCl2, 10 mM CaCl2 |
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| 染色 | タイプ: NEGATIVE 詳細: Protein complexes were adsorbed to antibody-decorated microchips for 2 minutes and stained with 1% uranyl formate for 1 minute. |
| グリッド | 詳細: SiN microchips with TEM windows coated with 25% Ni-NTA functionalized lipid monolayers |
| 凍結 | 凍結剤: NONE / 装置: OTHER |
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電子顕微鏡法
| 顕微鏡 | FEI TECNAI SPIRIT |
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| 温度 | 最低: 83 K |
| アライメント法 | Legacy - 非点収差: Objective lens astigmatism was corrected at high magnification. |
| 詳細 | low-dose illumination |
| 日付 | 2015年3月23日 |
| 撮影 | カテゴリ: CCD / フィルム・検出器のモデル: FEI EAGLE (2k x 2k) / デジタル化 - サンプリング間隔: 30 µm / 実像数: 129 / 平均電子線量: 5 e/Å2 |
| 電子線 | 加速電圧: 120 kV / 電子線源: LAB6 |
| 電子光学系 | 倍率(補正後): 75000 / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2 mm / 最大 デフォーカス(公称値): -3.0 µm / 最小 デフォーカス(公称値): -1.0 µm / 倍率(公称値): 68000 |
| 試料ステージ | 試料ホルダーモデル: GATAN LIQUID NITROGEN |
| 実験機器 | ![]() モデル: Tecnai Spirit / 画像提供: FEI Company |
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画像解析
| 詳細 | The particles were selected using an automatic selection program. |
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| 最終 再構成 | アルゴリズム: OTHER / 解像度のタイプ: BY AUTHOR / 解像度: 26.0 Å / 解像度の算出法: OTHER / ソフトウェア - 名称: RELION / 使用した粒子像数: 3000 |
| 最終 2次元分類 | クラス数: 1 |
-原子モデル構築 1
| 初期モデル | PDB ID: Chain - #0 - Chain ID: A / Chain - #1 - Chain ID: B / Chain - #2 - Chain ID: C / Chain - #3 - Chain ID: D / Chain - #4 - Chain ID: E / Chain - #5 - Chain ID: F / Chain - #6 - Chain ID: G / Chain - #7 - Chain ID: H / Chain - #8 - Chain ID: I / Chain - #9 - Chain ID: J / Chain - #10 - Chain ID: K / Chain - #11 - Chain ID: L |
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| ソフトウェア | 名称: Chimera |
| 詳細 | The domains were separately fitted by manual docking using the Chimera software package. |
| 精密化 | 空間: REAL / プロトコル: RIGID BODY FIT |
-原子モデル構築 2
| 初期モデル | PDB ID: Chain - Chain ID: A |
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| ソフトウェア | 名称: Chimera |
| 詳細 | The domains were separately fitted by manual docking using the Chimera software package. |
| 精密化 | 空間: REAL / プロトコル: RIGID BODY FIT |
-原子モデル構築 3
| 初期モデル | PDB ID: Chain - #0 - Chain ID: A / Chain - #1 - Chain ID: B |
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| ソフトウェア | 名称: Chimera |
| 詳細 | The domains were separately fitted by manual docking using the Chimera software package. |
| 精密化 | 空間: REAL / プロトコル: RIGID BODY FIT |
-原子モデル構築 4
| 初期モデル | PDB ID: Chain - Chain ID: A |
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| ソフトウェア | 名称: Chimera |
| 詳細 | This domain was used to generate a homology based model using the program SWISS-MODEL. |
| 精密化 | 空間: REAL / プロトコル: RIGID BODY FIT |
ムービー
コントローラー
万見について



キーワード
Homo sapiens (ヒト)
データ登録者
引用
UCSF Chimera





































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