3zf4

Phage dUTPases control transfer of virulence genes by a proto- oncogenic G protein-like mechanism. (Staphylococcus bacteriophage 80alpha dUTPase Y81A mutant with dUpNHpp).

spinqualitylabelsall models 3zf4, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zf4 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: DUP, MG, NI Related: 3zez, 3zf0, 3zf1, 3zf2, 3zf3, 3zf5, 3zf6 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Deoxyuridine 5'-triphosphate nucleotidohydrolase

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