1rh6: Difference between revisions
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==Bacteriophage Lambda Excisionase (Xis)-DNA Complex== | |||
=== | <StructureSection load='1rh6' size='340' side='right' caption='[[1rh6]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1rh6]] is a 4 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RH6 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xis ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Enterobacteria phage lambda])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rh6 RCSB], [http://www.ebi.ac.uk/pdbsum/1rh6 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:15066428</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterobacteria phage lambda]] | [[Category: Enterobacteria phage lambda]] | ||
[[Category: Cascio, D | [[Category: Cascio, D]] | ||
[[Category: Clubb, R T | [[Category: Clubb, R T]] | ||
[[Category: Johnson, R C | [[Category: Johnson, R C]] | ||
[[Category: Sam, M D | [[Category: Sam, M D]] | ||
[[Category: Winged -helix protein]] | [[Category: Winged -helix protein]] | ||
[[Category: Dna architectural protein]] | [[Category: Dna architectural protein]] | ||
Revision as of 22:37, 3 January 2015
Bacteriophage Lambda Excisionase (Xis)-DNA Complex
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