Reserved Sandbox 329: Difference between revisions
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== '''Uridylyl transferases''' == | |||
[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg|thumb|left|upright=2.0|alt=Secondary Structure Succession of ATP-bound TUTases. Secondary structure residues are ordered from blue to red.|Secondary structure succession of ATP-bound TUTases.]] | |||
== 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 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}} | ||
== ''' | == STRUCTURE == | ||
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 catalyzing this reaction. | |||
== REFERENCES == | |||
<references/> | |||
== External Links == | |||
[http://www.rcsb.org/pdb/explore/explore.do?structureId=2Q0D RCSB Protein Data Bank] | |||
