1RXM
C-terminal region of FEN-1 bound to A. fulgidus PCNA
Summary for 1RXM
| Entry DOI | 10.2210/pdb1rxm/pdb |
| Related | 1RWZ 1RXV 1RXW 1RXZ |
| Descriptor | DNA polymerase sliding clamp, consensus FEN-1 peptide (3 entities in total) |
| Functional Keywords | sliding clamp, torus, processivity factor, beta-zipper, hydrophobic anchor, replication |
| Biological source | Archaeoglobus fulgidus More |
| Total number of polymer chains | 2 |
| Total formula weight | 28706.08 |
| Authors | Chapados, B.R.,Hosfield, D.J.,Han, S.,Qiu, J.,Yelent, B.,Shen, B.,Tainer, J.A. (deposition date: 2003-12-18, release date: 2004-01-27, Last modification date: 2023-08-23) |
| Primary citation | 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 Cited by 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: 14718165DOI: 10.1016/S0092-8674(03)01036-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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