1rh6

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[[Image:1rh6.gif|left|200px]]<br /><applet load="1rh6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rh6.gif|left|200px]]
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caption="1rh6, resolution 1.70&Aring;" />
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'''Bacteriophage Lambda Excisionase (Xis)-DNA Complex'''<br />
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{{Structure
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|PDB= 1rh6 |SIZE=350|CAPTION= <scene name='initialview01'>1rh6</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= xis ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Enterobacteria phage lambda])
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}}
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'''Bacteriophage Lambda Excisionase (Xis)-DNA Complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RH6 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=1RH6 OCA].
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1RH6 is a [[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=1RH6 OCA].
==Reference==
==Reference==
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Crystal structure of the excisionase-DNA complex from bacteriophage lambda., Sam MD, Cascio D, Johnson RC, Clubb RT, J Mol Biol. 2004 Apr 23;338(2):229-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15066428 15066428]
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Crystal structure of the excisionase-DNA complex from bacteriophage lambda., Sam MD, Cascio D, Johnson RC, Clubb RT, J Mol Biol. 2004 Apr 23;338(2):229-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15066428 15066428]
[[Category: Enterobacteria phage lambda]]
[[Category: Enterobacteria phage lambda]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Johnson, R C.]]
[[Category: Johnson, R C.]]
[[Category: Sam, M D.]]
[[Category: Sam, M D.]]
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[[Category: 'winged'-helix protein]]
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[[Category: winged -helix protein]]
[[Category: dna architectural protein]]
[[Category: dna architectural protein]]
[[Category: phage excision]]
[[Category: phage excision]]
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[[Category: site-specific dna recombination]]
[[Category: site-specific dna recombination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:51:35 2008''

Revision as of 11:51, 20 March 2008


PDB ID 1rh6

Drag the structure with the mouse to rotate
, resolution 1.70Å
Gene: xis (Enterobacteria phage lambda)
Coordinates: save as pdb, mmCIF, xml



Bacteriophage Lambda Excisionase (Xis)-DNA Complex


Overview

The excisionase (Xis) protein from bacteriophage lambda is the best characterized member of a large family of recombination directionality factors that control integrase-mediated DNA rearrangements. It triggers phage excision by cooperatively binding to sites X1 and X2 within the phage, bending DNA significantly and recruiting the phage-encoded integrase (Int) protein to site P2. We have determined the co-crystal structure of Xis with its X2 DNA-binding site at 1.7A resolution. Xis forms a unique winged-helix motif that interacts with the major and minor grooves of its binding site using an alpha-helix and an ordered beta-hairpin (wing), respectively. Recognition is achieved through an elaborate water-mediated hydrogen-bonding network at the major groove interface, while the preformed hairpin forms largely non-specific interactions with the minor groove. The structure of the complex provides insights into how Xis recruits Int cooperatively, and suggests a plausible mechanism by which it may distort longer DNA fragments significantly. It reveals a surface on the protein that is likely to mediate Xis-Xis interactions required for its cooperative binding to DNA.

About this Structure

1RH6 is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

Reference

Crystal structure of the excisionase-DNA complex from bacteriophage lambda., Sam MD, Cascio D, Johnson RC, Clubb RT, J Mol Biol. 2004 Apr 23;338(2):229-40. PMID:15066428

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