3zf3: Difference between revisions
New page: '''Unreleased structure''' The entry 3zf3 is ON HOLD Authors: Tormo-Mas, M.A., Donderis, J., Garcia-Caballer, M., Alt, A., Mir-Sanchis, I., Marina, A., Penades, J.R. Description: Phage... |
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==Phage dUTPases control transfer of virulence genes by a proto-oncogenic G protein-like mechanism. (Staphylococcus bacteriophage 80alpha dUTPase Y84I mutant).== | |||
<StructureSection load='3zf3' size='340' side='right'caption='[[3zf3]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zf3]] 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=3ZF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZF3 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]] 3.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3zf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zf3 OCA], [https://pdbe.org/3zf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zf3 RCSB], [https://www.ebi.ac.uk/pdbsum/3zf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zf3 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zf3" 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]] |