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1rxw

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[[Image:1rxw.gif|left|200px]]
[[Image:1rxw.gif|left|200px]]
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{{Structure
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|PDB= 1rxw |SIZE=350|CAPTION= <scene name='initialview01'>1rxw</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1rxw", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
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|ACTIVITY=
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|GENE= FEN, AF0264 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
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|DOMAIN=
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{{STRUCTURE_1rxw| PDB=1rxw | SCENE= }}
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|RELATEDENTRY=[[1rxv|1RXV]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxw OCA], [http://www.ebi.ac.uk/pdbsum/1rxw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rxw RCSB]</span>
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}}
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'''Crystal structure of A. fulgidus FEN-1 bound to DNA'''
'''Crystal structure of A. fulgidus FEN-1 bound to DNA'''
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[[Category: Yelent, B.]]
[[Category: Yelent, B.]]
[[Category: 3' flap binding site]]
[[Category: 3' flap binding site]]
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[[Category: helical clamp]]
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[[Category: Helical clamp]]
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[[Category: helix-3 turn-helix]]
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[[Category: Helix-3 turn-helix]]
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[[Category: hydrophobic wedge]]
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[[Category: Hydrophobic wedge]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:02:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:34:34 2008''
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Revision as of 05:02, 3 May 2008

Template:STRUCTURE 1rxw

Crystal structure of A. fulgidus FEN-1 bound to DNA


Overview

Flap EndoNuclease-1 (FEN-1) and the processivity factor proliferating cell nuclear antigen (PCNA) are central to DNA replication and repair. To clarify the molecular basis of FEN-1 specificity and PCNA activation, we report here structures of FEN-1:DNA and PCNA:FEN-1-peptide complexes, along with fluorescence resonance energy transfer (FRET) and mutational results. FEN-1 binds the unpaired 3' DNA end (3' flap), opens and kinks the DNA, and promotes conformational closing of a flexible helical clamp to facilitate 5' cleavage specificity. Ordering of unstructured C-terminal regions in FEN-1 and PCNA creates an intermolecular beta sheet interface that directly links adjacent PCNA and DNA binding regions of FEN-1 and suggests how PCNA stimulates FEN-1 activity. The DNA and protein conformational changes, composite complex structures, FRET, and mutational results support enzyme-PCNA alignments and a kinked DNA pivot point that appear suitable to coordinate rotary handoffs of kinked DNA intermediates among enzymes localized by the three PCNA binding sites.

About this Structure

1RXW is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair., Chapados BR, Hosfield DJ, Han S, Qiu J, Yelent B, Shen B, Tainer JA, Cell. 2004 Jan 9;116(1):39-50. PMID:14718165 Page seeded by OCA on Sat May 3 08:02:24 2008

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