1p7d

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(New page: 200px<br /><applet load="1p7d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p7d, resolution 2.95&Aring;" /> '''Crystal structure of...)
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[[Image:1p7d.gif|left|200px]]<br /><applet load="1p7d" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1p7d.gif|left|200px]]<br /><applet load="1p7d" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p7d, resolution 2.95&Aring;" />
caption="1p7d, resolution 2.95&Aring;" />
'''Crystal structure of the Lambda Integrase (residues 75-356) bound to DNA'''<br />
'''Crystal structure of the Lambda Integrase (residues 75-356) bound to DNA'''<br />
==Overview==
==Overview==
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The bacteriophage lambda integrase protein (lambda Int) belongs to a, family of tyrosine recombinases that catalyze DNA rearrangements. We have, determined a crystal structure of lambda Int complexed with a cleaved DNA, substrate through a covalent phosphotyrosine bond. In comparison to an, earlier unliganded structure, we observe a drastic conformational change, in DNA-bound lambda Int that brings Tyr342 into the active site for, cleavage of the DNA in cis. A flexible linker connects the central and the, catalytic domains, allowing the protein to encircle the DNA. Binding, specificity is achieved through direct interactions with the DNA and, indirect readout of the flexibility of the att site. The conformational, switch that activates lambda Int for DNA cleavage exposes the C-terminal 8, residues for interactions with a neighboring Int molecule. The protein, interactions mediated by lambda Int's C-terminal tail offer a mechanism, for the allosteric control of cleavage activity in higher order lambda Int, complexes.
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The bacteriophage lambda integrase protein (lambda Int) belongs to a family of tyrosine recombinases that catalyze DNA rearrangements. We have determined a crystal structure of lambda Int complexed with a cleaved DNA substrate through a covalent phosphotyrosine bond. In comparison to an earlier unliganded structure, we observe a drastic conformational change in DNA-bound lambda Int that brings Tyr342 into the active site for cleavage of the DNA in cis. A flexible linker connects the central and the catalytic domains, allowing the protein to encircle the DNA. Binding specificity is achieved through direct interactions with the DNA and indirect readout of the flexibility of the att site. The conformational switch that activates lambda Int for DNA cleavage exposes the C-terminal 8 residues for interactions with a neighboring Int molecule. The protein interactions mediated by lambda Int's C-terminal tail offer a mechanism for the allosteric control of cleavage activity in higher order lambda Int complexes.
==About this Structure==
==About this Structure==
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1P7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P7D OCA].
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1P7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P7D OCA].
==Reference==
==Reference==
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[[Category: Aihara, H.]]
[[Category: Aihara, H.]]
[[Category: Ellenberger, T.]]
[[Category: Ellenberger, T.]]
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[[Category: Kwon, H.J.]]
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[[Category: Kwon, H J.]]
[[Category: Landy, A.]]
[[Category: Landy, A.]]
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[[Category: Nunes-Duby, S.E.]]
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[[Category: Nunes-Duby, S E.]]
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:32:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:55 2008''

Revision as of 12:25, 21 February 2008


1p7d, resolution 2.95Å

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Crystal structure of the Lambda Integrase (residues 75-356) bound to DNA

Overview

The bacteriophage lambda integrase protein (lambda Int) belongs to a family of tyrosine recombinases that catalyze DNA rearrangements. We have determined a crystal structure of lambda Int complexed with a cleaved DNA substrate through a covalent phosphotyrosine bond. In comparison to an earlier unliganded structure, we observe a drastic conformational change in DNA-bound lambda Int that brings Tyr342 into the active site for cleavage of the DNA in cis. A flexible linker connects the central and the catalytic domains, allowing the protein to encircle the DNA. Binding specificity is achieved through direct interactions with the DNA and indirect readout of the flexibility of the att site. The conformational switch that activates lambda Int for DNA cleavage exposes the C-terminal 8 residues for interactions with a neighboring Int molecule. The protein interactions mediated by lambda Int's C-terminal tail offer a mechanism for the allosteric control of cleavage activity in higher order lambda Int complexes.

About this Structure

1P7D is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

Reference

A conformational switch controls the DNA cleavage activity of lambda integrase., Aihara H, Kwon HJ, Nunes-Duby SE, Landy A, Ellenberger T, Mol Cell. 2003 Jul;12(1):187-98. PMID:12887904

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