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1b43
From Proteopedia
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| - | [[Image:1b43.gif|left|200px]] | + | [[Image:1b43.gif|left|200px]] |
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| - | '''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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| , 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
Page seeded by OCA on Thu Mar 20 10:05:58 2008
