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==Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domainm.==
==Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domainm.==
<StructureSection load='2qy2' size='340' side='right' caption='[[2qy2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2qy2' size='340' side='right'caption='[[2qy2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qy2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mimivirus Mimivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QY2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2qy2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mimivirus Mimivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QY2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qze|2qze]], [[3bgy|3bgy]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Refseq YP_142736 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=315393 Mimivirus])</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=2qy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qy2 OCA], [https://pdbe.org/2qy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qy2 RCSB], [https://www.ebi.ac.uk/pdbsum/2qy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qy2 ProSAT]</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=2qy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qy2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qy2 RCSB], [http://www.ebi.ac.uk/pdbsum/2qy2 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MCE_MIMIV MCE_MIMIV]] Responsible for methylating the 5'-cap structure of mRNAs.  
[https://www.uniprot.org/uniprot/MCE_MIMIV MCE_MIMIV] Responsible for methylating the 5'-cap structure of mRNAs.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The RNA triphosphatase (RTPase) components of the mRNA capping apparatus are a bellwether of eukaryal taxonomy. Fungal and protozoal RTPases belong to the triphosphate tunnel metalloenzyme (TTM) family, exemplified by yeast Cet1. Several large DNA viruses encode metal-dependent RTPases unrelated to the cysteinyl-phosphatase RTPases of their metazoan host organisms. The origins of DNA virus RTPases are unclear because they are structurally uncharacterized. Mimivirus, a giant virus of amoeba, resembles poxviruses in having a trifunctional capping enzyme composed of a metal-dependent RTPase module fused to guanylyltransferase (GTase) and guanine-N7 methyltransferase domains. The crystal structure of mimivirus RTPase reveals a minimized tunnel fold and an active site strikingly similar to that of Cet1. Unlike homodimeric fungal RTPases, mimivirus RTPase is a monomer. The mimivirus TTM-type RTPase-GTase fusion resembles the capping enzymes of amoebae, providing evidence that the ancestral large DNA virus acquired its capping enzyme from a unicellular host.
 
Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain.,Benarroch D, Smith P, Shuman S Structure. 2008 Apr;16(4):501-12. PMID:18400173<ref>PMID:18400173</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mimivirus]]
[[Category: Mimivirus]]
[[Category: Benarroch, D]]
[[Category: Benarroch D]]
[[Category: Shuman, S]]
[[Category: Shuman S]]
[[Category: Smith, P]]
[[Category: Smith P]]
[[Category: Beta tunnel]]
[[Category: Hydrolase]]
[[Category: Mrna capping]]
[[Category: Mrna processing]]
[[Category: Multifunctional enzyme]]
[[Category: Nucleotidyltransferase]]
[[Category: Phosphatase]]
[[Category: S-adenosyl-l-methionine]]
[[Category: Transferase]]
[[Category: Viral protein]]
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