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1b43

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(New page: 200px<br /><applet load="1b43" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b43, resolution 2.0&Aring;" /> '''FEN-1 FROM P. FURIOSU...)
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[[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==
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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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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==
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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].
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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]]
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[[Category: Hosfield, D.J.]]
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[[Category: Hosfield, D J.]]
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[[Category: Mol, C.D.]]
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[[Category: Mol, C D.]]
[[Category: Shen, B.]]
[[Category: Shen, B.]]
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[[Category: Tainer, J.A.]]
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[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:20:26 2007''
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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 09:51, 21 February 2008


1b43, resolution 2.0Å

Drag the structure with the mouse to rotate

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 Feb 21 11:51:18 2008

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