1xns
From Proteopedia
(New page: 200px<br /><applet load="1xns" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xns, resolution 2.80Å" /> '''Peptide trapped Holl...) |
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| - | [[Image:1xns.gif|left|200px]]<br /><applet load="1xns" size=" | + | [[Image:1xns.gif|left|200px]]<br /><applet load="1xns" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xns, resolution 2.80Å" /> | caption="1xns, resolution 2.80Å" /> | ||
'''Peptide trapped Holliday junction intermediate in Cre-loxP recombination'''<br /> | '''Peptide trapped Holliday junction intermediate in Cre-loxP recombination'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cre recombinase is a prototypical member of the tyrosine recombinase | + | Cre recombinase is a prototypical member of the tyrosine recombinase family of site-specific recombinases. Members of this family of enzymes catalyze recombination between specific DNA sequences by cleaving and exchanging one pair of strands between the two substrate sites to form a 4-way Holliday junction (HJ) intermediate and then resolve the HJ intermediate to recombinant products by a second round of strand exchanges. Recently, hexapeptide inhibitors have been described that are capable of blocking the second strand exchange step in the tyrosine recombinase recombination pathway, leading to an accumulation of the HJ intermediate. These peptides are active in the lambda-integrase, Cre recombinase, and Flp recombinase systems and are potentially important tools for both in vitro mechanistic studies and as in vivo probes of cellular function. Here we present biochemical and crystallographic data that support a model where the peptide inhibitor binds in the center of the recombinase-bound DNA junction and interacts with solvent-exposed bases near the junction branch point. Peptide binding induces large conformational changes in the DNA strands of the HJ intermediate, which affect the active site geometries in the recombinase subunits. |
==About this Structure== | ==About this Structure== | ||
| - | 1XNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http:// | + | 1XNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Enterobacteria phage p21]] | [[Category: Enterobacteria phage p21]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Duyne, G | + | [[Category: Duyne, G D.Van.]] |
[[Category: Ghosh, K.]] | [[Category: Ghosh, K.]] | ||
[[Category: Guo, F.]] | [[Category: Guo, F.]] | ||
| - | [[Category: Lau, C | + | [[Category: Lau, C K.]] |
| - | [[Category: Segall, A | + | [[Category: Segall, A M.]] |
[[Category: complex (recombinase/dna)]] | [[Category: complex (recombinase/dna)]] | ||
[[Category: cre recombinase]] | [[Category: cre recombinase]] | ||
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[[Category: recombination]] | [[Category: recombination]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:47 2008'' |
Revision as of 13:56, 21 February 2008
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Peptide trapped Holliday junction intermediate in Cre-loxP recombination
Overview
Cre recombinase is a prototypical member of the tyrosine recombinase family of site-specific recombinases. Members of this family of enzymes catalyze recombination between specific DNA sequences by cleaving and exchanging one pair of strands between the two substrate sites to form a 4-way Holliday junction (HJ) intermediate and then resolve the HJ intermediate to recombinant products by a second round of strand exchanges. Recently, hexapeptide inhibitors have been described that are capable of blocking the second strand exchange step in the tyrosine recombinase recombination pathway, leading to an accumulation of the HJ intermediate. These peptides are active in the lambda-integrase, Cre recombinase, and Flp recombinase systems and are potentially important tools for both in vitro mechanistic studies and as in vivo probes of cellular function. Here we present biochemical and crystallographic data that support a model where the peptide inhibitor binds in the center of the recombinase-bound DNA junction and interacts with solvent-exposed bases near the junction branch point. Peptide binding induces large conformational changes in the DNA strands of the HJ intermediate, which affect the active site geometries in the recombinase subunits.
About this Structure
1XNS is a Single protein structure of sequence from Enterobacteria phage p21. Full crystallographic information is available from OCA.
Reference
Peptide trapping of the Holliday junction intermediate in Cre-loxP site-specific recombination., Ghosh K, Lau CK, Guo F, Segall AM, Van Duyne GD, J Biol Chem. 2005 Mar 4;280(9):8290-9. Epub 2004 Dec 8. PMID:15591069
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