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 2.8&Aring;" /> '''C-terminal region of ...)
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[[Image:1rxm.gif|left|200px]]<br /><applet load="1rxm" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rxm.gif|left|200px]]<br /><applet load="1rxm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rxm, resolution 2.8&Aring;" />
caption="1rxm, resolution 2.8&Aring;" />
'''C-terminal region of FEN-1 bound to A. fulgidus PCNA'''<br />
'''C-terminal region of FEN-1 bound to A. fulgidus PCNA'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1RXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RXM OCA].
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1RXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXM OCA].
==Reference==
==Reference==
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[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chapados, B.R.]]
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[[Category: Chapados, B R.]]
[[Category: Han, S.]]
[[Category: Han, S.]]
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[[Category: Hosfield, D.J.]]
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[[Category: Hosfield, D J.]]
[[Category: Qiu, J.]]
[[Category: Qiu, J.]]
[[Category: Shen, B.]]
[[Category: Shen, B.]]
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[[Category: Tainer, J.A.]]
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[[Category: Tainer, J A.]]
[[Category: Yelent, B.]]
[[Category: Yelent, B.]]
[[Category: beta-zipper]]
[[Category: beta-zipper]]
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[[Category: torus]]
[[Category: torus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:56:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:37 2008''

Revision as of 12:55, 21 February 2008


1rxm, resolution 2.8Å

Drag the structure with the mouse to rotate

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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