1lx8: Difference between revisions

Revision as of 22:45, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lx8.png

Template:STRUCTURE 1lx8

Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis proteinRegulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein

Template:ABSTRACT PUBMED 12460578

About this StructureAbout this Structure

1LX8 is a Single protein structure of sequence from Enterobacteria phage lambda. Full experimental information is available from OCA.

ReferenceReference

Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein., Sam MD, Papagiannis CV, Connolly KM, Corselli L, Iwahara J, Lee J, Phillips M, Wojciak JM, Johnson RC, Clubb RT, J Mol Biol. 2002 Dec 6;324(4):791-805. PMID:12460578

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-'''Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein'''
+===Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein===
-==Overview==
+<!--
-Upon induction of a bacteriophage lambda lysogen, a site-specific recombination reaction excises the phage genome from the chromosome of its bacterial host. A critical regulator of this process is the phage-encoded excisionase (Xis) protein, which functions both as a DNA architectural factor and by cooperatively recruiting integrase to an adjacent binding site specifically required for excision. Here we present the three-dimensional structure of Xis and the results of a structure-based mutagenesis study to define the molecular basis of its function. Xis adopts an unusual "winged"-helix motif that is modeled to interact with the major- and minor-grooves of its binding site through a single alpha-helix and loop structure ("wing"), respectively. The C-terminal tail of Xis, which is required for cooperative binding with integrase, is unstructured in the absence of DNA. We propose that asymmetric bending of DNA by Xis positions its unstructured C-terminal tail for direct contacts with the N-terminal DNA-binding domain of integrase and that an ensuing disordered to ordered transition of the tail may act to stabilize the formation of the tripartite integrase-Xis-DNA complex required for phage excision.
+The line below this paragraph, {{ABSTRACT_PUBMED_12460578}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12460578 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12460578}}
 ==About this Structure==
-LX8 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=1LX8 OCA].
+LX8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LX8 OCA].
 ==Reference==
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 [[Category: Phage excision]]
 [[Category: Site-specific dna recombination]]
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