1rxv: Difference between revisions

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[[Image:1rxv.gif|left|200px]]<br /><applet load="1rxv" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1rxv.gif|left|200px]]<br /><applet load="1rxv" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1rxv, resolution 2.5Å" />

'''Crystal Structure of A. Fulgidus FEN-1 bound to DNA'''<br />

==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.

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==

1RXV 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=1RXV OCA].

1RXV 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=1RXV OCA].

==Reference==

Line 13:

[[Category: Archaeoglobus fulgidus]]

[[Category: Single protein]]

[[Category: Chapados, B.R.]]

[[Category: Chapados, B R.]]

[[Category: Han, S.]]

[[Category: Hosfield, D.J.]]

[[Category: Hosfield, D J.]]

[[Category: Qiu, J.]]

[[Category: Shen, B.]]

[[Category: Tainer, J.A.]]

[[Category: Tainer, J A.]]

[[Category: Yelent, B.]]

[[Category: 3' flap binding site]]

Line 27:

[[Category: protein-dna complex]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:41 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1rxv.gif|left|200px]]<br /><applet load="1rxv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rxv.gif|left|200px]]<br /><applet load="1rxv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rxv, resolution 2.5&Aring;" />
 '''Crystal Structure of A. Fulgidus FEN-1 bound to DNA'''<br />
 ==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.
+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==
-RXV 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=1RXV OCA].
+RXV 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=1RXV OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Archaeoglobus fulgidus]]
 [[Category: Single protein]]
-[[Category: Chapados, B.R.]]
+[[Category: Chapados, B R.]]
 [[Category: Han, S.]]
-[[Category: Hosfield, D.J.]]
+[[Category: Hosfield, D J.]]
 [[Category: Qiu, J.]]
 [[Category: Shen, B.]]
-[[Category: Tainer, J.A.]]
+[[Category: Tainer, J A.]]
 [[Category: Yelent, B.]]
 [[Category: 3' flap binding site]]
@@ Line 27: / Line 27: @@
 [[Category: protein-dna complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:56:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:41 2008''