4p37
From Proteopedia
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| - | ''' | + | ==Crystal structure of the Megavirus polyadenylate synthase== |
| + | <StructureSection load='4p37' size='340' side='right' caption='[[4p37]], [[Resolution|resolution]] 2.24Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4p37]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P37 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4p37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p37 RCSB], [http://www.ebi.ac.uk/pdbsum/4p37 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:25779049</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Abergel, C]] | ||
| + | [[Category: Claverie, J M]] | ||
[[Category: Lartigue, A]] | [[Category: Lartigue, A]] | ||
| - | [[Category: Claverie, J.M]] | ||
[[Category: Priet, S]] | [[Category: Priet, S]] | ||
| - | [[Category: | + | [[Category: Polya polymerase]] |
| + | [[Category: Transferase]] | ||
Revision as of 13:11, 1 April 2015
Crystal structure of the Megavirus polyadenylate synthase
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