- EMDB-42289: Cryo-EM map of human clamp-clamp loader ATAD5-RFC-cracked PCNA co... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-42289
タイトル
Cryo-EM map of human clamp-clamp loader ATAD5-RFC-cracked PCNA complex in intermediate state 2
マップデータ
Final sharpened Cryo-EM map
試料
複合体: ATAD5-RFC-cracked PCNA
タンパク質・ペプチド: ATPase family AAA domain-containing protein 5
タンパク質・ペプチド: Replication factor C subunit 2
タンパク質・ペプチド: Replication factor C subunit 5
タンパク質・ペプチド: Replication factor C subunit 4
タンパク質・ペプチド: Replication factor C subunit 3
タンパク質・ペプチド: Proliferating cell nuclear antigen
リガンド: MAGNESIUM ION
リガンド: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
リガンド: ADENOSINE-5'-DIPHOSPHATE
キーワード
AAA ATPase / Clamp unloader / MOTOR PROTEIN
機能・相同性
機能・相同性情報
DNA clamp unloader activity / positive regulation of cell cycle G2/M phase transition / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / response to organophosphorus / Ctf18 RFC-like complex / DNA clamp loader activity / nuclear DNA replication / DNA replication factor C complex ...DNA clamp unloader activity / positive regulation of cell cycle G2/M phase transition / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / response to organophosphorus / Ctf18 RFC-like complex / DNA clamp loader activity / nuclear DNA replication / DNA replication factor C complex / Elg1 RFC-like complex / mitotic telomere maintenance via semi-conservative replication / purine-specific mismatch base pair DNA N-glycosylase activity / positive regulation of isotype switching to IgG isotypes / nuclear lamina / MutLalpha complex binding / positive regulation of DNA-directed DNA polymerase activity / Polymerase switching / Telomere C-strand (Lagging Strand) Synthesis / Processive synthesis on the lagging strand / PCNA complex / Removal of the Flap Intermediate / Processive synthesis on the C-strand of the telomere / isotype switching / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Polymerase switching on the C-strand of the telomere / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Transcription of E2F targets under negative control by DREAM complex / Removal of the Flap Intermediate from the C-strand / replisome / Activation of ATR in response to replication stress / regulation of mitotic cell cycle phase transition / DNA duplex unwinding / response to L-glutamate / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / DNA strand elongation involved in DNA replication / histone acetyltransferase binding / DNA synthesis involved in DNA repair / DNA polymerase processivity factor activity / positive regulation of DNA replication / G1/S-Specific Transcription / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / replication fork processing / response to dexamethasone / leading strand elongation / nuclear replication fork / cyclin-dependent protein kinase holoenzyme complex / Presynaptic phase of homologous DNA pairing and strand exchange / SUMOylation of DNA replication proteins / estrous cycle / epithelial cell differentiation / PCNA-Dependent Long Patch Base Excision Repair / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / signal transduction in response to DNA damage / positive regulation of DNA repair / ATP-dependent activity, acting on DNA / mismatch repair / male germ cell nucleus / translesion synthesis / response to cadmium ion / DNA polymerase binding / positive regulation of B cell proliferation / liver regeneration / Translesion synthesis by REV1 / Translesion synthesis by POLK / base-excision repair, gap-filling / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / replication fork / nuclear estrogen receptor binding / Recognition of DNA damage by PCNA-containing replication complex / Termination of translesion DNA synthesis / G2/M DNA damage checkpoint / Translesion Synthesis by POLH / HDR through Homologous Recombination (HRR) / Dual Incision in GG-NER / DNA-templated DNA replication / receptor tyrosine kinase binding / cellular response to hydrogen peroxide / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / cellular response to xenobiotic stimulus / cellular response to UV / Processing of DNA double-strand break ends / E3 ubiquitin ligases ubiquitinate target proteins / response to estradiol / heart development / chromosome, telomeric region / DNA replication / Regulation of TP53 Activity through Phosphorylation / cell population proliferation / damaged DNA binding / nuclear body / DNA repair / chromatin binding / centrosome / chromatin / protein-containing complex binding 類似検索 - 分子機能
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM131754
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM115809
米国
Howard Hughes Medical Institute (HHMI)
米国
引用
ジャーナル: Nat Struct Mol Biol / 年: 2024 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.