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<StructureSection load='3pkz' size='340' side='right'caption='[[3pkz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3pkz' size='340' side='right'caption='[[3pkz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3pkz]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PKZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3pkz]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PKZ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2r0q|2r0q]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sin, SAP013A_018, SAP095A_006, SAP096A_020 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=3pkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pkz OCA], [https://pdbe.org/3pkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pkz RCSB], [https://www.ebi.ac.uk/pdbsum/3pkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pkz 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=3pkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pkz OCA], [https://pdbe.org/3pkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pkz RCSB], [https://www.ebi.ac.uk/pdbsum/3pkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pkz ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/BIN3_STAAU BIN3_STAAU] Potential DNA invertase.
Sin resolvase is a site-specific serine recombinase that is normally controlled by a complex regulatory mechanism. A single mutation, Q115R, allows the enzyme to bypass the entire regulatory apparatus, such that no accessory proteins or DNA sites are required. Here, we present a 1.86 A crystal structure of the Sin Q115R catalytic domain, in a tetrameric arrangement stabilized by an interaction between Arg115 residues on neighboring subunits. The subunits have undergone significant conformational changes from the inactive dimeric state previously reported. The structure provides a new high-resolution view of a serine recombinase active site that is apparently fully assembled, suggesting roles for the conserved active site residues. The structure also suggests how the dimer-tetramer transition is coupled to assembly of the active site. The tetramer is captured in a different rotational substate than that seen in previous hyperactive serine recombinase structures, and unbroken crossover site DNA can be readily modeled into its active sites.
 
Structural basis for catalytic activation of a serine recombinase.,Keenholtz RA, Rowland SJ, Boocock MR, Stark WM, Rice PA Structure. 2011 Jun 8;19(6):799-809. PMID:21645851<ref>PMID:21645851</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3pkz" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Resolvase 3D structures|Resolvase 3D structures]]
*[[Resolvase 3D structures|Resolvase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Boocock, M R]]
[[Category: Staphylococcus aureus]]
[[Category: Keenholtz, R A]]
[[Category: Boocock MR]]
[[Category: Rice, P A]]
[[Category: Keenholtz RA]]
[[Category: Rowland, S J]]
[[Category: Rice PA]]
[[Category: Stark, W M]]
[[Category: Rowland SJ]]
[[Category: Dna]]
[[Category: Stark WM]]
[[Category: Recombination]]
[[Category: Resolvase]]
[[Category: Small serine recombinase]]

Latest revision as of 10:41, 21 February 2024

Structural basis for catalytic activation of a serine recombinase

3pkz, resolution 1.80Å

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