Literature summary for 1.14.11.47 extracted from

Chowdhury, R.; Sekirnik, R.; Brissett, N.; Krojer, T.; Ho, C.; Ng, S.; Clifton, I.; Ge, W.; Kershaw, N.; Fox, G.; Muniz, J.; Vollmar, M.; Phillips, C.; Pilka, E.; Kavanagh, K.; von Delft, F.; Oppermann, U.; McDonough, M.; Doherty, A.; Schofield, C.
Ribosomal oxygenases are structurally conserved from prokaryotes to humans (2014), Nature, 510, 422-426.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.6 A resolution. Comparison with crystal structures of human MYC-induced nuclear antigen MINA53 and nucleolar protein NO66 as well as Rhodothermus marinus YcfD. The observed modes of ribosomal oxygenases hydroxylations have probably evolved into those of other JmjC-containing hydroxylases and the histoneNepsilon-methyl lysine demethylases, both by altering the coordination position from which the ferryl-oxo reacts and by engineering the depth of substrate penetration	Escherichia coli

Crystallization (Comment)

Organism

to 2.6 A resolution. Comparison with crystal structures of human MYC-induced nuclear antigen MINA53 and nucleolar protein NO66 as well as Rhodothermus marinus YcfD. The observed modes of ribosomal oxygenases hydroxylations have probably evolved into those of other JmjC-containing hydroxylases and the histoneNepsilon-methyl lysine demethylases, both by altering the coordination position from which the ferryl-oxo reacts and by engineering the depth of substrate penetration

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P27431	-	-

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Release 2023.1 (January 2023)