1b43
From Proteopedia
(New page: 200px<br /><applet load="1b43" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b43, resolution 2.0Å" /> '''FEN-1 FROM P. FURIOSU...) |
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| - | [[Image:1b43.gif|left|200px]]<br /><applet load="1b43" size=" | + | [[Image:1b43.gif|left|200px]]<br /><applet load="1b43" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b43, resolution 2.0Å" /> | caption="1b43, resolution 2.0Å" /> | ||
'''FEN-1 FROM P. FURIOSUS'''<br /> | '''FEN-1 FROM P. FURIOSUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Flap endonuclease (FEN-1) removes 5' overhanging flaps in DNA repair and | + | 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== | ==About this Structure== | ||
| - | 1B43 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http:// | + | 1B43 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hosfield, D | + | [[Category: Hosfield, D J.]] |
| - | [[Category: Mol, C | + | [[Category: Mol, C D.]] |
[[Category: Shen, B.]] | [[Category: Shen, B.]] | ||
| - | [[Category: Tainer, J | + | [[Category: Tainer, J A.]] |
[[Category: dna repair]] | [[Category: dna repair]] | ||
[[Category: dna replication]] | [[Category: dna replication]] | ||
[[Category: nuclease]] | [[Category: nuclease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:18 2008'' |
Revision as of 09:51, 21 February 2008
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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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