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-Structure paper
タイトル | The human ATAD5 has evolved unique structural elements to function exclusively as a PCNA unloader. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Year 2024 |
掲載日 | 2024年6月13日 |
著者 | Feng Wang / Qing He / Nina Y Yao / Michael E O'Donnell / Huilin Li / |
PubMed 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. |
リンク | Nat Struct Mol Biol / PubMed:38871854 |
手法 | EM (単粒子) |
解像度 | 3.04 - 4.2 Å |
構造データ | EMDB-42287, PDB-8ui7: EMDB-42288, PDB-8ui8: EMDB-42289, PDB-8ui9: EMDB-42295, PDB-8uii: |
化合物 | ChemComp-MG: ChemComp-AGS: ChemComp-ADP: |
由来 |
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キーワード | MOTOR PROTEIN / AAA ATPase / Clamp unloader |