2og0: Difference between revisions
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<StructureSection load='2og0' size='340' side='right'caption='[[2og0]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2og0' size='340' side='right'caption='[[2og0]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2og0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2og0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OG0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2og0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2og0 OCA], [https://pdbe.org/2og0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2og0 RCSB], [https://www.ebi.ac.uk/pdbsum/2og0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2og0 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2og0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2og0 OCA], [https://pdbe.org/2og0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2og0 RCSB], [https://www.ebi.ac.uk/pdbsum/2og0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2og0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VXIS_LAMBD VXIS_LAMBD] Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia virus Lambda]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Abbani | [[Category: Abbani MA]] | ||
[[Category: Cascio | [[Category: Cascio D]] | ||
[[Category: Clubb | [[Category: Clubb RT]] | ||
[[Category: Johnson | [[Category: Johnson RC]] | ||
[[Category: Papagiannis | [[Category: Papagiannis CV]] | ||
[[Category: Sam | [[Category: Sam MD]] | ||
[[Category: Yoo | [[Category: Yoo D]] | ||
Latest revision as of 16:09, 26 July 2023
Crystal Structure of the Lambda Xis-DNA complexCrystal Structure of the Lambda Xis-DNA complex
Structural highlights
FunctionVXIS_LAMBD Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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