1RXW

Crystal structure of A. fulgidus FEN-1 bound to DNA

1RXW の概要

• エントリーDOI: 10.2210/pdb1rxw/pdb
• 関連するPDBエントリー: 1RXV
• 分子名称: 5'-d(*C*pG*pA*pT*pG*pC*pT*pA)-3', 5'-d(*T*pA*pG*pC*pA*pT*pC*pG*pG)-3', Flap structure-specific endonuclease, ... (4 entities in total)
• 機能のキーワード: helical clamp, helix-3 turn-helix, hydrophobic wedge, 3' flap binding site, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Archaeoglobus fulgidus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43299.84

構造登録者

Chapados, B.R.,Hosfield, D.J.,Han, S.,Qiu, J.,Yelent, B.,Shen, B.,Tainer, J.A. (登録日: 2003-12-18, 公開日: 2004-01-27, 最終更新日: 2023-08-23)

主引用文献

Chapados, B.R.,Hosfield, D.J.,Han, S.,Qiu, J.,Yelent, B.,Shen, B.,Tainer, J.A.
Structural Basis for FEN-1 Substrate Specificity and PCNA-Mediated Activation in DNA Replication and Repair
Cell(Cambridge,Mass.), 116:39-50, 2004

PubMed Abstract: Flap EndoNuclease-1 (FEN-1) and the processivity factor proliferating cell nuclear antigen (PCNA) are central to DNA replication and repair. To clarify the molecular basis of FEN-1 specificity and PCNA activation, we report here structures of FEN-1:DNA and PCNA:FEN-1-peptide complexes, along with fluorescence resonance energy transfer (FRET) and mutational results. FEN-1 binds the unpaired 3' DNA end (3' flap), opens and kinks the DNA, and promotes conformational closing of a flexible helical clamp to facilitate 5' cleavage specificity. Ordering of unstructured C-terminal regions in FEN-1 and PCNA creates an intermolecular beta sheet interface that directly links adjacent PCNA and DNA binding regions of FEN-1 and suggests how PCNA stimulates FEN-1 activity. The DNA and protein conformational changes, composite complex structures, FRET, and mutational results support enzyme-PCNA alignments and a kinked DNA pivot point that appear suitable to coordinate rotary handoffs of kinked DNA intermediates among enzymes localized by the three PCNA binding sites.

PubMed: 14718165
DOI: 10.1016/S0092-8674(03)01036-5

実験手法

X-RAY DIFFRACTION (2 Å)