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Reserved Sandbox 329
From Proteopedia
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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> |
| - | The bound <scene name='Reserved_Sandbox_329/Ligand/4'> | + | {{STRUCTURE_2q0d | PDB=2q0d | SCENE=Reserved_Sandbox_329/Scene1/1}} |
| - | <scene name='Reserved_Sandbox_329/ | + | |
| - | <scene name='Reserved_Sandbox_329/ | + | == 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. | ||
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| + | == REFERENCES == | ||
| + | <references/> | ||
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| + | == External Links == | ||
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| + | [http://www.rcsb.org/pdb/explore/explore.do?structureId=2Q0D RCSB Protein Data Bank] | ||
Current revision
Contents |
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 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 Mg2+ ions.[1]
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| 2q0d, resolution 2.00Å () | |||||||||
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| Ligands: | , | ||||||||
| 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 with two Mg2+ ions, however many TUTases involved in RNA editing are shown to exhibit preference for binding to UTP instead.[1] Three are conserved in TUTases, and are required for coordinating the Mg2+ ions in some TUTases. [1] Thus, these are vital in catalyzing this reaction.
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
