1b43: Difference between revisions
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'''FEN-1 FROM P. FURIOSUS''' | '''FEN-1 FROM P. FURIOSUS''' | ||
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[[Category: Shen, B.]] | [[Category: Shen, B.]] | ||
[[Category: Tainer, J A.]] | [[Category: Tainer, J A.]] | ||
[[Category: | [[Category: Dna repair]] | ||
[[Category: | [[Category: Dna replication]] | ||
[[Category: | [[Category: Nuclease]] | ||
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Revision as of 08:02, 2 May 2008
FEN-1 FROM P. FURIOSUS
Overview
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.
About this Structure
1B43 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity., Hosfield DJ, Mol CD, Shen B, Tainer JA, Cell. 1998 Oct 2;95(1):135-46. PMID:9778254 Page seeded by OCA on Fri May 2 11:02:24 2008