1.14.11.47: [50S ribosomal protein L16]-arginine 3-hydroxylase

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For detailed information about [50S ribosomal protein L16]-arginine 3-hydroxylase, go to the full flat file.

Reaction

Synonyms

50S ribosomal protein L16 arginine hydroxylase, ycfD

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

                1.14.11.47 [50S ribosomal protein L16]-arginine 3-hydroxylase

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Results	in table
304	AA Sequence
1	Cloned(Commentary)
2	Crystallization (Commentary)
2	General Information
4	KM Value [mM]
1	Metals/Ions
1	Natural Substrates/ Products (Substrates)
6	Organism
9	PDB ID
3	Protein Variants
1	Reaction
6	Reference
15	Substrates and Products (Substrate)
6	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Stability [°C]
2	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.11.47 - [50S ribosomal protein L16]-arginine 3-hydroxylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

mutant E146A/K147A, predicted to enhance crystallizability, to 2.7 A resolution, space group P43212 with a single protein molecule in the asymmetric unit. The N-terminal domain contains the signature DSBH or beta-barrel that is characteristic of 2OG-dependent oxygenases. The core DSBH is made up of two beta-sheets, one composed of five strands and the second one composed of three strands

Escherichia coli

P27431

730216

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

P27431

730469