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| [[Image:2qze.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2qze| PDB=2qze | SCENE= }} | | {{STRUCTURE_2qze| PDB=2qze | SCENE= }} |
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| '''Monoclinic Mimivirus Capping Enzyme Triphosphatase.'''
| | ===Monoclinic Mimivirus Capping Enzyme Triphosphatase.=== |
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| ==Overview==
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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. | | The line below this paragraph, {{ABSTRACT_PUBMED_18400173}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18400173 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18400173}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tunnel]] | | [[Category: Tunnel]] |
| [[Category: Viral protein]] | | [[Category: Viral protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:27:58 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:59:13 2008'' |
