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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]] 2.00Å' scene=''> | + | <StructureSection load='2qy2' size='340' side='right'caption='[[2qy2]], [[Resolution|resolution]] 2.00Å' 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]] 2Å</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://pdbe.org/2qy2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qy2 RCSB], [http://www.ebi.ac.uk/pdbsum/2qy2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qy2 ProSAT]</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;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 2qy2" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| | __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]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Mrna capping]]
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| - | [[Category: Mrna processing]]
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| - | [[Category: Multifunctional enzyme]]
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| - | [[Category: Nucleotidyltransferase]]
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| - | [[Category: Phosphatase]]
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| - | [[Category: S-adenosyl-l-methionine]]
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| - | [[Category: Transferase]]
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| - | [[Category: Viral protein]]
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