1b43: Difference between revisions
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[[Image:1b43.gif|left|200px]] | [[Image:1b43.gif|left|200px]] | ||
'''FEN-1 FROM P. FURIOSUS''' | {{Structure | ||
|PDB= 1b43 |SIZE=350|CAPTION= <scene name='initialview01'>1b43</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''FEN-1 FROM P. FURIOSUS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1B43 is a [ | 1B43 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B43 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9778254 9778254] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nuclease]] | [[Category: nuclease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:05:58 2008'' | ||
Revision as of 08:05, 20 March 2008
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| 1b43, resolution 2.0Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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