3zf1: Difference between revisions

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==Phage dUTPases control transfer of virulence genes by a proto- oncogenic G protein-like mechanism. (Staphylococcus bacteriophage 80alpha dUTPase D81N mutant with dUpNHpp).==
==Phage dUTPases control transfer of virulence genes by a proto- oncogenic G protein-like mechanism. (Staphylococcus bacteriophage 80alpha dUTPase D81N mutant with dUpNHpp).==
<StructureSection load='3zf1' size='340' side='right' caption='[[3zf1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3zf1' size='340' side='right'caption='[[3zf1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3zf1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_80_alpha Bacteriophage 80 alpha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZF1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3zf1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_80_alpha Bacteriophage 80 alpha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZF1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DUP:2-DEOXYURIDINE+5-ALPHA,BETA-IMIDO-TRIPHOSPHATE'>DUP</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
</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=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zez|3zez]], [[3zf0|3zf0]], [[3zf2|3zf2]], [[3zf3|3zf3]], [[3zf4|3zf4]], [[3zf5|3zf5]], [[3zf6|3zf6]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zez|3zez]], [[3zf0|3zf0]], [[3zf2|3zf2]], [[3zf3|3zf3]], [[3zf4|3zf4]], [[3zf5|3zf5]], [[3zf6|3zf6]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] </span></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=3zf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zf1 OCA], [http://pdbe.org/3zf1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zf1 RCSB], [http://www.ebi.ac.uk/pdbsum/3zf1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zf1 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=3zf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zf1 OCA], [https://pdbe.org/3zf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zf1 RCSB], [https://www.ebi.ac.uk/pdbsum/3zf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zf1 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
*[[Deoxyuridine 5'-triphosphate nucleotidohydrolase|Deoxyuridine 5'-triphosphate nucleotidohydrolase]]
*[[DUTPase 3D structures|DUTPase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bacteriophage 80 alpha]]
[[Category: Bacteriophage 80 alpha]]
[[Category: Large Structures]]
[[Category: DUTP diphosphatase]]
[[Category: DUTP diphosphatase]]
[[Category: Alt, A]]
[[Category: Alt, A]]

Revision as of 08:44, 10 August 2022

Phage dUTPases control transfer of virulence genes by a proto- oncogenic G protein-like mechanism. (Staphylococcus bacteriophage 80alpha dUTPase D81N mutant with dUpNHpp).Phage dUTPases control transfer of virulence genes by a proto- oncogenic G protein-like mechanism. (Staphylococcus bacteriophage 80alpha dUTPase D81N mutant with dUpNHpp).

Structural highlights

3zf1 is a 1 chain structure with sequence from Bacteriophage 80 alpha. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:dUTP diphosphatase, with EC number 3.6.1.23
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

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

3zf1, resolution 3.00Å

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OCA