2qze: Difference between revisions
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New page: left|200px {{Structure |PDB= 2qze |SIZE=350|CAPTION= <scene name='initialview01'>2qze</scene>, resolution 2.90Å |SITE= |LIGAND= |ACTIVITY= |GENE= |DOMAIN= |R... |
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==Monoclinic Mimivirus Capping Enzyme Triphosphatase.== | |||
<StructureSection load='2qze' size='340' side='right'caption='[[2qze]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2qze]] 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=2QZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QZE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</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=2qze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qze OCA], [https://pdbe.org/2qze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qze RCSB], [https://www.ebi.ac.uk/pdbsum/2qze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qze ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 2qze" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mimivirus]] | [[Category: Mimivirus]] | ||
[[Category: Benarroch D]] | |||
[[Category: Benarroch | [[Category: Shuman S]] | ||
[[Category: Shuman | [[Category: Smith P]] | ||
[[Category: Smith | |||
Latest revision as of 11:43, 30 August 2023
Monoclinic Mimivirus Capping Enzyme Triphosphatase.
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