2ief: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of the cooperative Excisionase (Xis)-DNA complex reveals a micronucleoprotein filament== | ==Structure of the cooperative Excisionase (Xis)-DNA complex reveals a micronucleoprotein filament== | ||
<StructureSection load='2ief' size='340' side='right' caption='[[2ief]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2ief' size='340' side='right' caption='[[2ief]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| Line 4: | Line 5: | ||
<table><tr><td colspan='2'>[[2ief]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IEF FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ief]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IEF 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 Bacteriophage lambda])</td></tr> | </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 Bacteriophage 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=2ief FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ief OCA], [http://pdbe.org/2ief PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ief RCSB], [http://www.ebi.ac.uk/pdbsum/2ief PDBsum]</span></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=2ief FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ief OCA], [http://pdbe.org/2ief PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ief RCSB], [http://www.ebi.ac.uk/pdbsum/2ief PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ief ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Revision as of 10:55, 4 July 2018
Structure of the cooperative Excisionase (Xis)-DNA complex reveals a micronucleoprotein filamentStructure of the cooperative Excisionase (Xis)-DNA complex reveals a micronucleoprotein filament
Structural highlights
Function[VXIS_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 DNA architectural protein Xis regulates the construction of higher-order nucleoprotein intasomes that integrate and excise the genome of phage lambda from the Escherichia coli chromosome. Xis modulates the directionality of site-specific recombination by stimulating phage excision 10(6)-fold, while simultaneously inhibiting phage reintegration. Control is exerted by cooperatively assembling onto a approximately 35-bp DNA regulatory element, which it distorts to preferentially stabilize an excisive intasome. Here, we report the 2.6-A crystal structure of the complex between three cooperatively bound Xis proteins and a 33-bp DNA containing the regulatory element. Xis binds DNA in a head-to-tail orientation to generate a micronucleoprotein filament. Although each protomer is anchored to the duplex by a similar set of nonbase specific contacts, malleable protein-DNA interactions enable binding to sites that differ in nucleotide sequence. Proteins at the ends of the duplex sequence specifically recognize similar binding sites and participate in cooperative binding via protein-protein interactions with a bridging Xis protomer that is bound in a less specific manner. Formation of this polymer introduces approximately 72 degrees of curvature into the DNA with slight positive writhe, which functions to connect disparate segments of DNA bridged by integrase within the excisive intasome. Structure of the cooperative Xis-DNA complex reveals a micronucleoprotein filament that regulates phage lambda intasome assembly.,Abbani MA, Papagiannis CV, Sam MD, Cascio D, Johnson RC, Clubb RT Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2109-14. Epub 2007 Feb 7. PMID:17287355[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||