9B2D
Yeast Rad51-ssDNA filament
9B2D の概要
| エントリーDOI | 10.2210/pdb9b2d/pdb |
| EMDBエントリー | 44104 |
| 分子名称 | DNA repair protein RAD51, DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| 機能のキーワード | genome stability, recombination, rad51, dna repair, dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
| 由来する生物種 | Saccharomyces cerevisiae S288C (Baker's yeast) 詳細 |
| タンパク質・核酸の鎖数 | 7 |
| 化学式量合計 | 268512.54 |
| 構造登録者 | |
| 主引用文献 | Liu, J.,Gore, S.K.,Heyer, W.D. Local structural dynamics of Rad51 protomers revealed by cryo-electron microscopy of Rad51-ssDNA filaments. Nucleic Acids Res., 53:-, 2025 Cited by PubMed Abstract: Homologous recombination (HR) is a high-fidelity repair mechanism for double-strand breaks. Rad51 is the key enzyme that forms filaments on single-stranded DNA (ssDNA) to catalyze homology search and DNA strand exchange in recombinational DNA repair. In this study, we employed single-particle cryogenic electron microscopy (cryo-EM) to ascertain the density map of the wild-type budding yeast Rad51-ssDNA filament bound to ADP-AlF3, achieving a resolution of 2.35 Å without imposing helical symmetry. The model assigned 6 Rad51 protomers, 24 nt of DNA, and 6 bound ADP-AlF3. It shows 6-fold symmetry implying monomeric building blocks, unlike the structure of the Rad51-I345T mutant filament with three-fold symmetry implying dimeric building blocks, for which the structural comparisons provide a satisfying mechanistic explanation. This image analysis enables comprehensive comparisons of individual Rad51 protomers within the filament and reveals local conformational movements of amino acid side chains. Notably, R293 in Loop 1 adopts multiple conformations to facilitate L296 and V331 in separating and twisting the DNA triplets. We also analyzed the crystal structure of Rad51-I345T and the predicted structure of yeast Rad51-K342E using the Rad51-ssDNA structure from this study as a reference. PubMed: 39898551DOI: 10.1093/nar/gkaf052 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.4 Å) |
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