Reserved Sandbox 329: Difference between revisions
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== INTRODUCTION == | == INTRODUCTION == | ||
Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction | Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction that adds UMP to a RNA substrate. Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions.<ref name="primary citation">PMID:17785418</ref> | ||
{{STRUCTURE_2q0d | PDB=2q0d | SCENE=Reserved_Sandbox_329/Scene1/1}} | {{STRUCTURE_2q0d | PDB=2q0d | SCENE=Reserved_Sandbox_329/Scene1/1}} | ||
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== STRUCTURE == | == STRUCTURE == | ||
The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions | The uridylyl transferase bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions, however many TUTases involved in RNA editing are shown to exhibit preference for binding to UTP instead.<ref name="primary citation">PMID:17785418</ref> | ||
Three <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are conserved in TUTases, and are required for coordinating the Mg<sup>2+</sup> ions in some TUTases. <ref name="primary citation">PMID:17785418</ref> Thus, these <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are vital in catalysing this reaction. | |||
== REFERENCES == | == REFERENCES == | ||