1B43

FEN-1 FROM P. FURIOSUS

Summary for 1B43

• Entry DOI: 10.2210/pdb1b43/pdb
• Descriptor: PROTEIN (FEN-1) (2 entities in total)
• Functional Keywords: nuclease, dna repair, dna replication, transferase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 2
• Total formula weight: 77597.63

Authors

Hosfield, D.J.,Mol, C.D.,Shen, B.,Tainer, J.A. (deposition date: 1999-01-05, release date: 2000-01-12, Last modification date: 2023-12-27)

Primary citation

Hosfield, D.J.,Mol, C.D.,Shen, B.,Tainer, J.A.
Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity.
Cell(Cambridge,Mass.), 95:135-146, 1998

PubMed Abstract: Flap endonuclease (FEN-1) removes 5' overhanging flaps in DNA repair and processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. The crystal structure of Pyrococcus furiosus FEN-1, active-site metal ions, and mutational information indicate interactions for the single- and double-stranded portions of the flap DNA substrate and identify an unusual DNA-binding motif. The enzyme's active-site structure suggests that DNA binding induces FEN-1 to clamp onto the cleavage junction to form the productive complex. The conserved FEN-1 C terminus binds proliferating cell nuclear antigen (PCNA) and positions FEN-1 to act primarily as an exonuclease in DNA replication, in contrast to its endonuclease activity in DNA repair. FEN-1 mutations altering PCNA binding should reduce activity during replication, likely causing DNA repeat expansions as seen in some cancers and genetic diseases.

PubMed: 9778254
DOI: 10.1016/S0092-8674(00)81789-4

Experimental method

X-RAY DIFFRACTION (2 Å)