1b43: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1b43.gif|left|200px]]<br /><applet load="1b43" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1b43, resolution 2.0&Aring;" />
caption="1b43, resolution 2.0&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B43 OCA].  
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==
Line 13: Line 13:
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Hosfield, D.J.]]
[[Category: Hosfield, D J.]]
[[Category: Mol, C.D.]]
[[Category: Mol, C D.]]
[[Category: Shen, B.]]
[[Category: Shen, B.]]
[[Category: Tainer, J.A.]]
[[Category: Tainer, J A.]]
[[Category: dna repair]]
[[Category: dna repair]]
[[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 Thu Feb 21 11:51:18 2008''

Revision as of 12:51, 21 February 2008

File:1b43.gif


1b43, resolution 2.0Å

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FEN-1 FROM P. FURIOSUS

OverviewOverview

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 StructureAbout this Structure

1B43 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

ReferenceReference

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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