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==Constitutively active Sin recombinase cataltyic domain - I100T==
==Constitutively active Sin recombinase cataltyic domain - I100T==
<StructureSection load='5c32' size='340' side='right' caption='[[5c32]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
<StructureSection load='5c32' size='340' side='right'caption='[[5c32]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5c32]] is a 4 chain structure with sequence from [http://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=5C32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C32 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5c32]] is a 4 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=5C32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C32 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 3.053&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pkz|3pkz]], [[2r0q|2r0q]], [[5c31|5c31]], [[5c34|5c34]], [[5c35|5c35]]</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=5c32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c32 OCA], [https://pdbe.org/5c32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c32 RCSB], [https://www.ebi.ac.uk/pdbsum/5c32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c32 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bin3 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c32 OCA], [http://pdbe.org/5c32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c32 RCSB], [http://www.ebi.ac.uk/pdbsum/5c32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c32 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BIN3_STAAU BIN3_STAAU]] Potential DNA invertase.  
[https://www.uniprot.org/uniprot/BIN3_STAAU BIN3_STAAU] Potential DNA invertase.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Members of the serine family of site-specific recombinases exchange DNA strands via 180 degrees rotation about a central protein-protein interface. Modeling of this process has been hampered by the lack of structures in more than one rotational state for any individual serine recombinase. Here we report crystal structures of the catalytic domains of four constitutively active mutants of the serine recombinase Sin, providing snapshots of rotational states not previously visualized for Sin, including two seen in the same crystal. Normal mode analysis predicted that each tetramer's lowest frequency mode (i.e. most accessible large-scale motion) mimics rotation: two protomers rotate as a pair with respect to the other two. Our analyses also suggest that rotation is not a rigid body movement around a single symmetry axis but instead uses multiple pivot points and entails internal motions within each subunit.
 
Snapshots of a molecular swivel in action.,Trejo CS, Rock RS, Stark WM, Boocock MR, Rice PA Nucleic Acids Res. 2018 Jun 1;46(10):5286-5296. doi: 10.1093/nar/gkx1309. PMID:29315406<ref>PMID:29315406</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5c32" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Rice, P A]]
[[Category: Large Structures]]
[[Category: Trejo, C S]]
[[Category: Staphylococcus aureus]]
[[Category: Conformational flexibility]]
[[Category: Rice PA]]
[[Category: Dna binding protein]]
[[Category: Trejo CS]]
[[Category: Serine recombinase]]
[[Category: Site specific recombinase]]

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