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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. <scene name='Sandbox_Reserved_329/Tyr189/1'>tyrosine residue</scene>
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. <scene name='Sandbox_Reserved_329/Tyr189/1'>tyrosine residue</scene>
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<scene name='Sandbox_Reserved_329/Hydrophobic_hbond_interactions/1'>interactions</scene>
== REFERENCES ==
== REFERENCES ==

Revision as of 21:28, 29 March 2011

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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Contents

Uridylyl transferases

Secondary structure succession of ATP-bound TUTases.
Secondary structure succession of ATP-bound TUTases.

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]


PDB ID 2q0d

Drag the structure with the mouse to rotate
2q0d, resolution 2.00Å ()
Ligands: ,
Gene: TUT4 (Trypanosoma brucei)
Activity: RNA uridylyltransferase, with EC number 2.7.7.52
Related: 2ikf, 2nom
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. ↑ 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
  2. ↑ 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

External Links

RCSB Protein Data Bank

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