Literature summary for 1.14.11.42 extracted from

Kato, M.; Araiso, Y.; Noma, A.; Nagao, A.; Suzuki, T.; Ishitani, R.; Nureki, O.
Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification (2011), Nucleic Acids Res., 39, 1576-1585.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	A2RUC4	-	-

Synonyms

Synonyms	Comment	Organism
tRNA wybutosine-synthesizing protein 5	-	Homo sapiens
TYW5	-	Homo sapiens

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Release 2023.1 (January 2023)