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基本情報
登録情報 | データベース: PDB / ID: 8ui7 | ||||||||||||
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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 | ||||||||||||
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![]() | MOTOR PROTEIN / AAA ATPase / Clamp unloader | ||||||||||||
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 / purine-specific mismatch base pair DNA N-glycosylase activity / nuclear lamina / positive regulation of DNA-directed DNA polymerase activity / Polymerase switching / DNA clamp loader activity / Telomere C-strand (Lagging Strand) Synthesis / MutLalpha complex binding / 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 / Removal of the Flap Intermediate from the C-strand / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Transcription of E2F targets under negative control by DREAM complex / replisome / regulation of mitotic cell cycle phase transition / HDR through Single Strand Annealing (SSA) / response to L-glutamate / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / Impaired BRCA2 binding to RAD51 / DNA synthesis involved in DNA repair / DNA strand elongation involved in DNA replication / histone acetyltransferase binding / DNA polymerase processivity factor activity / leading strand elongation / G1/S-Specific Transcription / response to dexamethasone / 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 / translesion synthesis / mismatch repair / Activation of ATR in response to replication stress / response to cadmium ion / estrous cycle / cyclin-dependent protein kinase holoenzyme complex / base-excision repair, gap-filling / DNA polymerase binding / positive regulation of B cell proliferation / epithelial cell differentiation / male germ cell nucleus / positive regulation of DNA repair / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / Translesion synthesis by REV1 / Translesion synthesis by POLK / liver regeneration / Translesion synthesis by POLI / replication fork / Gap-filling DNA repair synthesis and ligation in GG-NER / positive regulation of DNA replication / nuclear estrogen receptor binding / Termination of translesion DNA synthesis / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH / G2/M DNA damage checkpoint / receptor tyrosine kinase binding / HDR through Homologous Recombination (HRR) / Dual Incision in GG-NER / cellular response to hydrogen peroxide / DNA-templated DNA replication / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / cellular response to UV / cellular response to xenobiotic stimulus / E3 ubiquitin ligases ubiquitinate target proteins / response to estradiol / heart development / Processing of DNA double-strand break ends / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / chromosome, telomeric region / cell population proliferation / DNA replication / nuclear body / DNA repair / centrosome / chromatin binding / protein-containing complex binding / chromatin / enzyme binding / negative regulation of transcription by RNA polymerase II 類似検索 - 分子機能 | ||||||||||||
生物種 | ![]() | ||||||||||||
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: 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
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 501.2 KB | 表示 | ![]() |
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PDB形式 | ![]() | 399.1 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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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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要素
-タンパク質 , 2種, 4分子 AFGH
#1: タンパク質 | 分子量: 116421.094 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: Insect cell expression vector pTIE1 (その他) 参照: UniProt: Q96QE3 |
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#6: タンパク質 | 分子量: 28795.752 Da / 分子数: 3 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: Insect cell expression vector pTIE1 (その他) 参照: UniProt: P12004 |
-Replication factor C subunit ... , 4種, 4分子 BCDE
#2: タンパク質 | 分子量: 39203.207 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: Insect cell expression vector pTIE1 (その他) 参照: UniProt: P35250 |
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#3: タンパク質 | 分子量: 38545.512 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: Insect cell expression vector pTIE1 (その他) 参照: UniProt: P40937 |
#4: タンパク質 | 分子量: 39735.711 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: Insect cell expression vector pTIE1 (その他) 参照: UniProt: P35249 |
#5: タンパク質 | 分子量: 40614.332 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: Insect cell expression vector pTIE1 (その他) 参照: UniProt: P40938 |
-非ポリマー , 3種, 8分子 




#7: 化合物 | #8: 化合物 | #9: 化合物 | |
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-詳細
研究の焦点であるリガンドがあるか | Y |
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Has protein modification | N |
-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 |
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試料調製
構成要素 | 名称: ATAD5-RFC-gapped PCNA / タイプ: COMPLEX / Entity ID: #1-#6 / 由来: RECOMBINANT |
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分子量 | 値: 0.32 MDa / 実験値: NO |
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: Insect cell expression vector pTIE1 (その他) |
緩衝液 | pH: 7.5 |
試料 | 濃度: 1 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
急速凍結 | 凍結剤: ETHANE |
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電子顕微鏡撮影
顕微鏡 | モデル: FEI TITAN |
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電子銃 | 電子線源: ![]() |
電子レンズ | モード: DIFFRACTION / 最大 デフォーカス(公称値): 2000 nm / 最小 デフォーカス(公称値): 1000 nm |
撮影 | 電子線照射量: 60 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
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解析
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3次元再構成 | 解像度: 4.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 55855 / 対称性のタイプ: POINT |