Reserved Sandbox 329: Difference between revisions
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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> 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. TUTases function in RNA editing; they add UMP to the 3' hydroxyl group.<ref name="primary citation">PMID:17785418</ref> | 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> 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. TUTases function in RNA editing; they add UMP to the 3' hydroxyl group.<ref name="primary citation">PMID:17785418</ref> | ||
== STRUCTURE == | |||
The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions. | The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions. | ||
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== | == REFERENCES == | ||
<references/> | <references/> | ||
