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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 | Cryo-EM map of human clmap-clamp loader ATAD5-RFC-gapped PCNA complex in intermediate state 3 | ||||||||||||
![]() | Final sharpen cryo-EM map | ||||||||||||
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![]() | AAA ATPase / Clamp unloader / MOTOR PROTEIN | ||||||||||||
機能・相同性 | ![]() DNA clamp unloader activity / positive regulation of cell cycle G2/M phase transition / Elg1 RFC-like complex / DNA replication factor C complex / Ctf18 RFC-like complex / nuclear DNA replication / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / mitotic telomere maintenance via semi-conservative replication ...DNA clamp unloader activity / positive regulation of cell cycle G2/M phase transition / Elg1 RFC-like complex / DNA replication factor C complex / Ctf18 RFC-like complex / nuclear DNA replication / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / mitotic telomere maintenance via semi-conservative replication / positive regulation of isotype switching to IgG isotypes / DNA clamp loader activity / purine-specific mismatch base pair DNA N-glycosylase activity / nuclear lamina / positive regulation of DNA-directed DNA polymerase activity / Polymerase switching / MutLalpha complex binding / Telomere C-strand (Lagging Strand) Synthesis / Processive synthesis on the lagging strand / PCNA complex / Removal of the Flap Intermediate / isotype switching / Processive synthesis on the C-strand of the telomere / Polymerase switching on the C-strand of the telomere / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Removal of the Flap Intermediate from the C-strand / Transcription of E2F targets under negative control by DREAM complex / replisome / response to L-glutamate / regulation of mitotic cell cycle phase transition / HDR through Single Strand Annealing (SSA) / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / Impaired BRCA2 binding to RAD51 / DNA strand elongation involved in DNA replication / response to dexamethasone / DNA synthesis involved in DNA repair / histone acetyltransferase binding / DNA polymerase processivity factor activity / leading strand elongation / G1/S-Specific Transcription / replication fork processing / nuclear replication fork / Presynaptic phase of homologous DNA pairing and strand exchange / SUMOylation of DNA replication proteins / signal transduction in response to DNA damage / PCNA-Dependent Long Patch Base Excision Repair / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / ATP-dependent activity, acting on DNA / response to cadmium ion / translesion synthesis / mismatch repair / estrous cycle / Activation of ATR in response to replication stress / cyclin-dependent protein kinase holoenzyme complex / Translesion synthesis by REV1 / Translesion synthesis by POLK / base-excision repair, gap-filling / DNA polymerase binding / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / positive regulation of B cell proliferation / epithelial cell differentiation / liver regeneration / positive regulation of DNA repair / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / Termination of translesion DNA synthesis / positive regulation of DNA replication / replication fork / Recognition of DNA damage by PCNA-containing replication complex / nuclear estrogen receptor binding / Translesion Synthesis by POLH / male germ cell nucleus / HDR through Homologous Recombination (HRR) / Dual Incision in GG-NER / G2/M DNA damage checkpoint / receptor tyrosine kinase binding / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / DNA-templated DNA replication / cellular response to hydrogen peroxide / cellular response to xenobiotic stimulus / cellular response to UV / E3 ubiquitin ligases ubiquitinate target proteins / response to estradiol / Processing of DNA double-strand break ends / heart development / chromatin organization / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / chromosome, telomeric region / DNA replication / cell population proliferation / nuclear body / DNA repair / centrosome / chromatin binding / chromatin / protein-containing complex binding / enzyme binding 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: 4.2 Å | ||||||||||||
![]() | Wang F / He Q / Li H | ||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: The human ATAD5 has evolved unique structural elements to function exclusively as a PCNA unloader. 著者: Feng Wang / Qing He / Nina Y Yao / Michael E O'Donnell / Huilin Li / ![]() 要旨: Humans have three different proliferating cell nuclear antigen (PCNA) clamp-loading complexes: RFC and CTF18-RFC load PCNA onto DNA, but ATAD5-RFC can only unload PCNA from DNA. The underlying ...Humans have three different proliferating cell nuclear antigen (PCNA) clamp-loading complexes: RFC and CTF18-RFC load PCNA onto DNA, but ATAD5-RFC can only unload PCNA from DNA. The underlying structural basis of ATAD5-RFC unloading is unknown. We show here that ATAD5 has two unique locking loops that appear to tie the complex into a rigid structure, and together with a domain that plugs the DNA-binding chamber, prevent conformation changes required for DNA binding, likely explaining why ATAD5-RFC is exclusively a PCNA unloader. These features are conserved in the yeast PCNA unloader Elg1-RFC. We observe intermediates in which PCNA bound to ATAD5-RFC exists as a closed planar ring, a cracked spiral or a gapped spiral. Surprisingly, ATAD5-RFC can open a PCNA gap between PCNA protomers 2 and 3, different from the PCNA protomers 1 and 3 gap observed in all previously characterized clamp loaders. | ||||||||||||
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 | ![]() | 117.8 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 26.7 KB 26.7 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 10.6 KB | 表示 | ![]() |
画像 | ![]() | 61.2 KB | ||
Filedesc metadata | ![]() | 7.7 KB | ||
その他 | ![]() ![]() ![]() ![]() | 111 MB 61.2 MB 116.1 MB 116.1 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 904.9 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 904.5 KB | 表示 | |
XML形式データ | ![]() | 19 KB | 表示 | |
CIF形式データ | ![]() | 24.7 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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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 | Final sharpen cryo-EM map | ||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 0.828 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
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試料の構成要素
+全体 : ATAD5-RFC-gapped PCNA
+超分子 #1: ATAD5-RFC-gapped PCNA
+分子 #1: ATPase family AAA domain-containing protein 5
+分子 #2: Replication factor C subunit 2
+分子 #3: Replication factor C subunit 5
+分子 #4: Replication factor C subunit 4
+分子 #5: Replication factor C subunit 3
+分子 #6: Proliferating cell nuclear antigen
+分子 #7: MAGNESIUM ION
+分子 #8: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
+分子 #9: 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
濃度 | 1.0 mg/mL |
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緩衝液 | pH: 7.5 |
凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | FEI TITAN |
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撮影 | フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 平均電子線量: 60.0 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: DIFFRACTION / 最大 デフォーカス(公称値): 2.0 µm / 最小 デフォーカス(公称値): 1.0 µm |
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画像解析
初期モデル | モデルのタイプ: NONE |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 4.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 55855 |
初期 角度割当 | タイプ: RANDOM ASSIGNMENT |
最終 角度割当 | タイプ: RANDOM ASSIGNMENT |