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| {{STRUCTURE_1rxv| PDB=1rxv | SCENE= }} | | {{STRUCTURE_1rxv| PDB=1rxv | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14718165}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14718165 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14718165}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Helix-3 turn-helix]] | | [[Category: Helix-3 turn-helix]] |
| [[Category: Protein-dna complex]] | | [[Category: Protein-dna complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:02:25 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:38:23 2008'' |
