1rxm
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(New page: 200px<br /><applet load="1rxm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rxm, resolution 2.8Å" /> '''C-terminal region of ...)
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Revision as of 23:48, 20 November 2007
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C-terminal region of FEN-1 bound to A. fulgidus PCNA
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
1RXM 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
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