5u96: Difference between revisions

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-'''Unreleased structure'''
-The entry 5u96 is ON HOLD  until Paper Publication
+==Crystal structure of the coiled-coil domain from Listeria Innocua (Tetragonal Form)==
+<StructureSection load='5u96' size='340' side='right' caption='[[5u96]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5u96]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U96 FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uae|5uae]]</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=5u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u96 OCA], [http://pdbe.org/5u96 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u96 RCSB], [http://www.ebi.ac.uk/pdbsum/5u96 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u96 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Serine integrases catalyze the integration of bacteriophage DNA into a host genome by site-specific recombination between 'attachment sites' in the phage (attP) and the host (attB). The reaction is highly directional; the reverse excision reaction between the product attL and attR sites does not occur in the absence of a phage-encoded factor, nor does recombination occur between other pairings of attachment sites. A mechanistic understanding of how these enzymes achieve site-selectivity and directionality has been limited by a lack of structural models. Here, we report the structure of the C-terminal domains of a serine integrase bound to an attP DNA half-site. The structure leads directly to models for understanding how the integrase-bound attP and attB sites differ, why these enzymes preferentially form attP x attB synaptic complexes to initiate recombination, and how attL x attR recombination is prevented. In these models, different domain organizations on attP vs. attB half-sites allow attachment-site specific interactions to form between integrase subunits via an unusual protruding coiled-coil motif. These interactions are used to preferentially synapse integrase-bound attP and attB and inhibit synapsis of integrase-bound attL and attR. The results provide a structural framework for understanding, testing and engineering serine integrase function.
-Authors: Gupta, K., Van Duyne, G.D., Sharp, R., Yuan, J.B.
+Attachment site recognition and regulation of directionality by the serine integrases.,Rutherford K, Yuan P, Perry K, Sharp R, Van Duyne GD Nucleic Acids Res. 2013 Sep 1;41(17):8341-56. doi: 10.1093/nar/gkt580. Epub 2013 , Jul 2. PMID:23821671<ref>PMID:23821671</ref>
-Description: Crystal structure of the coiled-coil domain from Listeria Innocua (Tetragonal Form)
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5u96" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Duyne, G D.Van]]
 [[Category: Gupta, K]]
 [[Category: Sharp, R]]
-[[Category: Yuan, J.B]]
+[[Category: Yuan, J B]]
-[[Category: Van Duyne, G.D]]
+[[Category: Coiled-coil]]
+[[Category: Recombination]]
+[[Category: Site-specific recombination]]