View source for 3zf5


==Phage dUTPases control transfer of virulence genes by a proto-oncogenic G protein-like mechanism. (Staphylococcus bacteriophage 80alpha dUTPase Y84F mutant with dUpNHpp).==
<StructureSection load='3zf5' size='340' side='right'caption='[[3zf5]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zf5]] 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=3ZF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZF5 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DUP:2-DEOXYURIDINE+5-ALPHA,BETA-IMIDO-TRIPHOSPHATE'>DUP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=3zf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zf5 OCA], [https://pdbe.org/3zf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zf5 RCSB], [https://www.ebi.ac.uk/pdbsum/3zf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zf5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4ZF98_9CAUD A4ZF98_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
dUTPases (Duts) have emerged as promising regulatory molecules controlling relevant cellular processes. However, the mechanism underlying this regulatory function remains enigmatic. Using staphylococcal pathogenicity island (SaPI) repression as a model, we report here that phage Duts induce the transfer of SaPI-encoded virulence factors by switching between active (dUTP-bound) and inactive (apo state) conformations, a conversion catalyzed by their intrinsic dUTPase activity. Crystallographic and mutagenic analyses demonstrate that binding to dUTP reorders the C-terminal motif V of the phage-encoded Duts, rendering these proteins into the active conformation required for SaPI derepression. By contrast, the conversion to the apo state conformation by hydrolysis of the bound dUTP generates a protein that is unable to induce the SaPI cycle. Because none of the requirements involving Duts in SaPI transfer are exclusive to the phage-encoded proteins, we propose that Duts are widespread cellular regulators acting in a manner analogous to the eukaryotic G proteins.

Phage dUTPases Control Transfer of Virulence Genes by a Proto-Oncogenic G Protein-like Mechanism.,Tormo-Mas MA, Donderis J, Garcia-Caballer M, Alt A, Mir-Sanchis I, Marina A, Penades JR Mol Cell. 2013 Jan 15. pii: S1097-2765(12)01049-0. doi:, 10.1016/j.molcel.2012.12.013. PMID:23333307<ref>PMID:23333307</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zf5" 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: Alt A]]
[[Category: Donderis J]]
[[Category: Garcia-Caballer M]]
[[Category: Marina A]]
[[Category: Mir-Sanchis I]]
[[Category: Penades JR]]
[[Category: Tormo-Mas MA]]