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1b43

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[[Image:1b43.gif|left|200px]]
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{{Seed}}
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[[Image:1b43.png|left|200px]]
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{{STRUCTURE_1b43| PDB=1b43 | SCENE= }}
{{STRUCTURE_1b43| PDB=1b43 | SCENE= }}
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'''FEN-1 FROM P. FURIOSUS'''
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===FEN-1 FROM P. FURIOSUS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9778254 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9778254}}
==About this Structure==
==About this Structure==
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[[Category: Dna replication]]
[[Category: Dna replication]]
[[Category: Nuclease]]
[[Category: Nuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:12:13 2008''

Revision as of 15:12, 30 June 2008

Image:1b43.png

Template:STRUCTURE 1b43

FEN-1 FROM P. FURIOSUS

Template:ABSTRACT PUBMED 9778254

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 Mon Jun 30 18:12:13 2008

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