2og0: Difference between revisions

Revision as of 12:56, 28 July 2008

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File:2og0.png

Template:STRUCTURE 2og0

Crystal Structure of the Lambda Xis-DNA complexCrystal Structure of the Lambda Xis-DNA complex

Template:ABSTRACT PUBMED 17275024

About this StructureAbout this Structure

2OG0 is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

ReferenceReference

Fis targets assembly of the Xis nucleoprotein filament to promote excisive recombination by phage lambda., Papagiannis CV, Sam MD, Abbani MA, Yoo D, Cascio D, Clubb RT, Johnson RC, J Mol Biol. 2007 Mar 23;367(2):328-43. Epub 2007 Jan 3. PMID:17275024

Page seeded by OCA on Mon Jul 28 12:56:07 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2og0.gif|left|200px]]
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 {{STRUCTURE_2og0|  PDB=2og0  |  SCENE=  }}
-'''Crystal Structure of the Lambda Xis-DNA complex'''
+===Crystal Structure of the Lambda Xis-DNA complex===
-==Overview==
+<!--
-The phage-encoded Xis protein is the major determinant controlling the direction of recombination in phage lambda. Xis is a winged-helix DNA binding protein that cooperatively binds to the attR recombination site to generate a curved microfilament, which promotes assembly of the excisive intasome but inhibits formation of an integrative intasome. We find that lambda synthesizes surprisingly high levels of Xis immediately upon prophage induction when excision rates are maximal. However, because of its low sequence-specific binding activity, exemplified by a 1.9 A co-crystal structure of a non-specifically bound DNA complex, Xis is relatively ineffective at promoting excision in vivo in the absence of the host Fis protein. Fis binds to a segment in attR that almost entirely overlaps one of the Xis binding sites. Instead of sterically excluding Xis binding from this site, as has been previously believed, we show that Fis enhances binding of all three Xis protomers to generate the microfilament. A specific Fis-Xis interface is supported by the effects of mutations within each protein, and relaxed, but not completely sequence-neutral, binding by the central Xis protomer is supported by the effects of DNA mutations. We present a structural model for the 50 bp curved Fis-Xis cooperative complex that is assembled between the arm and core Int binding sites whose trajectory places constraints on models for the excisive intasome structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_17275024}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17275024}}
 ==About this Structure==
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 [[Category: Protein-dna complex]]
 [[Category: Site-specific recombination recombination]]
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