View source for 5cco


==Staphylococcus bacteriophage 80alpha dUTPase with dUMP.==
<StructureSection load='5cco' size='340' side='right'caption='[[5cco]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cco]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_virus_80alpha Staphylococcus virus 80alpha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CCO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></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=5cco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cco OCA], [https://pdbe.org/5cco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cco RCSB], [https://www.ebi.ac.uk/pdbsum/5cco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cco ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4ZF98_9CAUD A4ZF98_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have recently proposed that the trimeric staphylococcal phage encoded dUTPases (Duts) are signaling molecules that act analogously to eukaryotic G-proteins, using dUTP as a second messenger. To perform this regulatory role, the Duts require their characteristic extra motif VI, present in all the staphylococcal phage coded trimeric Duts, as well as the strongly conserved Dut motif V. Recently, however, an alternative model involving Duts in the transfer of the staphylococcal islands (SaPIs) has been suggested, questioning the implication of motifs V and VI. Here, using state-of the-art techniques, we have revisited the proposed models. Our results confirm that the mechanism by which the Duts derepress the SaPI cycle depends on dUTP and involves both motifs V and VI, as we have previously proposed. Surprisingly, the conserved Dut motif IV is also implicated in SaPI derepression. However, and in agreement with the proposed alternative model, the dUTP inhibits rather than inducing the process, as we had initially proposed. In summary, our results clarify, validate and establish the mechanism by which the Duts perform regulatory functions.

Another look at the mechanism involving trimeric dUTPases in Staphylococcus aureus pathogenicity island induction involves novel players in the party.,Maiques E, Quiles-Puchalt N, Donderis J, Ciges-Tomas JR, Alite C, Bowring JZ, Humphrey S, Penades JR, Marina A Nucleic Acids Res. 2016 Apr 25. pii: gkw317. PMID:27112567<ref>PMID:27112567</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cco" style="background-color:#fffaf0;"></div>

==See Also==
*[[DUTPase 3D structures|DUTPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus virus 80alpha]]
[[Category: Alite C]]
[[Category: Bowring J]]
[[Category: Ciges JR]]
[[Category: Donderis J]]
[[Category: Maiques E]]
[[Category: Marina A]]
[[Category: Penades JR]]
[[Category: Quiles-Puchalt N]]