Reserved Sandbox 329

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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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[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg|left|400px|Secondary Structure Succession of ATP-bound TUTases]]
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[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg|thumb|center|upright=2.0|alt=Secondary Structure Succession of ATP-bound TUTases|Secondary Structure Succession of ATP-bound TUTases.]]

Revision as of 19:15, 16 March 2011

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



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] Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg2+ ions. TUTases function in RNA editing; they add UMP to the 3' hydroxyl group.[1]

STRUCTURE

The bound ligand is an with two Mg2+ ions.

Secondary Structure Succession of ATP-bound TUTases.
Secondary Structure Succession of ATP-bound TUTases.



REFERENCES

  1. 1.0 1.1 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

Proteopedia Page Contributors and Editors (what is this?)

Jessica Lowry

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