4p37 | pdb_00004p37

Crystal structure of the Megavirus polyadenylate synthase

spinqualitylabelsall models 4p37, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p37 is a 2 chain structure with sequence from Megavirus chiliensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.24Å Ligands: ALY, EDO, MSE, PEG, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G5CT11_9VIRU Publication Abstract from PubMed Giant viruses from the Mimiviridae family replicate entirely in their host cytoplasm where their genes are transcribed by a viral transcription apparatus. mRNA polyadenylation uniquely occurs at hairpin-forming palindromic sequences terminating viral transcripts. Here we show that a conserved gene cluster both encode the enzyme responsible for the hairpin cleavage and the viral polyA polymerases (vPAP). Unexpectedly, the vPAPs are homodimeric and uniquely self-processive. The vPAP backbone structures exhibit a symmetrical architecture with two subdomains sharing a nucleotidyltransferase topology, suggesting that vPAPs originate from an ancestral duplication. A Poxvirus processivity factor homologue encoded by Megavirus chilensis displays a conserved 5'-GpppA 2'O methyltransferase activity but is also able to internally methylate the mRNAs' polyA tails. These findings elucidate how the arm wrestling between hosts and their viruses to access the translation machinery is taking place in Mimiviridae. mRNA maturation in giant viruses: variation on a theme.,Priet S, Lartigue A, Debart F, Claverie JM, Abergel C Nucleic Acids Res. 2015 Mar 16. pii: gkv224. PMID:25779049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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