1RXZ

C-terminal region of A. fulgidus FEN-1 complexed with A. fulgidus PCNA

Summary for 1RXZ

• Entry DOI: 10.2210/pdb1rxz/pdb
• Related: 1RWZ 1RXM 1RXV 1RXW
• Descriptor: DNA polymerase sliding clamp, Flap structure-specific endonuclease (3 entities in total)
• Functional Keywords: beta-zipper, interdomain connecting loop, dna repair, dna replication, replication
• Biological source: Archaeoglobus fulgidus; More
• Total number of polymer chains: 2
• Total formula weight: 28670.06

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

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

Experimental method

X-RAY DIFFRACTION (2 Å)