Literature summary for 2.1.1.190 extracted from

Lee, T.T.; Agarwalla, S.; Stroud, R.M.
Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase (2004), Structure, 12, 397-407.

Search for more literature for 2.1.1.190

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, the crystal structure is determined at 1.95 A resolution using a single crystal of the selenomethionyl protein. The protein is organized into three structural domains. The N-terminal domain (residues 1574) is the smallest domain and is composed of five beta strands. The central domain (residues 7592 and 125262) and the catalytic domain (residues 93124 and 263431) are juxtaposed, and a concave surface is formed at the interface between them	Escherichia coli

Crystallization (Comment)

Organism

hanging drop vapor diffusion method, the crystal structure is determined at 1.95 A resolution using a single crystal of the selenomethionyl protein. The protein is organized into three structural domains. The N-terminal domain (residues 1574) is the smallest domain and is composed of five beta strands. The central domain (residues 7592 and 125262) and the catalytic domain (residues 93124 and 263431) are juxtaposed, and a concave surface is formed at the interface between them

Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	the central domain contains a [Fe4S4] cluster coordinated by four conserved cysteine residues. The iron-sulfur cluster may be involved in the correct folding of the protein or may have a role in RNA binding	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P55135	-	-

Synonyms

Synonyms	Comment	Organism
RumA	-	Escherichia coli

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Release 2023.1 (January 2023)