1ae9: Difference between revisions

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New page: left|200px<br /><applet load="1ae9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ae9, resolution 1.9Å" /> '''STRUCTURE OF THE LAMB...
 
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[[Image:1ae9.gif|left|200px]]<br /><applet load="1ae9" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ae9.gif|left|200px]]<br /><applet load="1ae9" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ae9, resolution 1.9&Aring;" />
caption="1ae9, resolution 1.9&Aring;" />
'''STRUCTURE OF THE LAMBDA INTEGRASE CATALYTIC CORE'''<br />
'''STRUCTURE OF THE LAMBDA INTEGRASE CATALYTIC CORE'''<br />


==Overview==
==Overview==
Lambda integrase is archetypic of site-specific recombinases that catalyze, intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent, phosphotyrosine intermediate in which Tyr342 is attached to the, 3'-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of, the integrase catalytic domain reveals a protein fold that is conserved in, organisms ranging from archaebacteria to yeast and that suggests a model, for interaction with target DNA. The attacking Tyr342 nucleophile is, located on a flexible loop about 20 angstroms from a basic groove that, contains all the other catalytically essential residues. This bipartite, active site can account for several apparently paradoxical features of, integrase family recombinases, including the capacity for both cis and, trans cleavage of DNA.
Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr342 is attached to the 3'-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr342 nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA.


==About this Structure==
==About this Structure==
1AE9 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=1AE9 OCA].  
1AE9 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=1AE9 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ellenberger, T.]]
[[Category: Ellenberger, T.]]
[[Category: Kwon, H.J.]]
[[Category: Kwon, H J.]]
[[Category: Landy, A.]]
[[Category: Landy, A.]]
[[Category: Tirumalai, R.]]
[[Category: Tirumalai, R.]]
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[[Category: site-specific recombination]]
[[Category: site-specific recombination]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:47:31 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:32 2008''

Revision as of 12:43, 21 February 2008

File:1ae9.gif


1ae9, resolution 1.9Å

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STRUCTURE OF THE LAMBDA INTEGRASE CATALYTIC CORE

OverviewOverview

Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr342 is attached to the 3'-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr342 nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA.

About this StructureAbout this Structure

1AE9 is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

ReferenceReference

Flexibility in DNA recombination: structure of the lambda integrase catalytic core., Kwon HJ, Tirumalai R, Landy A, Ellenberger T, Science. 1997 Apr 4;276(5309):126-31. PMID:9082984

Page seeded by OCA on Thu Feb 21 11:43:32 2008

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