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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 | 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 can function in RNA editing; more specifically TUTase4 catalyzes a reaction that adds a uridine monophosphate (UMP) from UTP 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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| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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Uridylyl transferases
INTRODUCTION
Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.[1] TUTases have been isolated from Trypanosoma brucei and also Leishmania ssp, parasites causing diseases in humans such as African Sleeping Sickness.[2] TUTases can function in RNA editing; more specifically TUTase4 catalyzes a reaction that adds a uridine monophosphate (UMP) from UTP 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 Mg2+ ions.[1]
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| 2q0d, resolution 2.00Å (default scene) | |||||||||||||
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| Ligands: | ATP, MG | ||||||||||||
| Gene: | TUT4 (Trypanosoma brucei) | ||||||||||||
| Activity: | RNA uridylyltransferase, with EC number 2.7.7.52 | ||||||||||||
| Related: | 2ikf, 2nom | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE
The uridylyl transferase bound ligand is an ATP complex with two Mg2+ ions, however many TUTases involved in RNA editing are shown to exhibit preference for binding to UTP instead.[1] Three aspartate residues are conserved in TUTases, and are required for coordinating the Mg2+ ions in some TUTases. [1] Thus, these aspartate residues are vital in catalyzing this reaction. tyrosine residue interactions
REFERENCES
- ↑ 1.0 1.1 1.2 1.3 Stagno J, Aphasizheva I, Aphasizhev R, Luecke H. Dual role of the RNA substrate in selectivity and catalysis by terminal uridylyl transferases. Proc Natl Acad Sci U S A. 2007 Sep 11;104(37):14634-9. Epub 2007 Sep 4. PMID:17785418
- ↑ Aphasizhev R, Sbicego S, Peris M, Jang SH, Aphasizheva I, Simpson AM, Rivlin A, Simpson L. Trypanosome mitochondrial 3' terminal uridylyl transferase (TUTase): the key enzyme in U-insertion/deletion RNA editing. Cell. 2002 Mar 8;108(5):637-48. PMID:11893335
