1.14.11.42: tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase

This is an abbreviated version!
For detailed information about tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase, go to the full flat file.

Reaction

7-(3-amino-3-carboxypropyl)wyosine37 in tRNAPhe
+
2-oxoglutarate
+
O2
=
7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe
+
succinate
+
CO2

Synonyms

tRNA wybutosine-synthesizing protein 5, tRNA yW-synthesizing enzyme 5, TYW5

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.42 tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase

Crystallization

Crystallization on EC 1.14.11.42 - tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the free and complex forms with 2-oxoglutarate and Ni(II) ion at 2.5 and 2.8 A resolution, respectively. The catalytic domain consists of a beta-jellyroll fold. The enzyme forms a homodimer through C-terminal helix bundle formation, thereby presenting a large, positively charged patch involved in tRNA binding. In a docking model of the TYW5-tRNAPhe complex, the D arm is captured by the positively charged patch, and the anticodon loop is directed into the positively charged catalytic pocket
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