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Literature summary for 2.1.1.172 extracted from

  • Sunita, S.; Purta, E.; Durawa, M.; Tkaczuk, K.L.; Swaathi, J.; Bujnicki, J.M.; Sivaraman, J.
    Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC (2007), Nucleic Acids Res., 35, 4264-4274.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
the rsmC gene, cloned into pCA24N vector with a noncleavable N-terminal His6 tag Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, crystal structure of RsmC refined to 2.1 A resolution, reveals two homologous domains tandemly duplicated within a single polypeptide. Characterization of the function of the individual domains and identification of key residues involved in binding of rRNA and S-adenosyl-L-methionine, and in catalysis. It is discovered that one of the domains is important for the folding of the other. RsmC can be regarded as a model system for functional streamlining of domains accompanied by the development of dependencies concerning folding and stability Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + guanine1207 in 16S rRNA Escherichia coli
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S-adenosyl-L-homocysteine + N2-methylguanine1207 in 16S rRNA
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P39406
-
-

Purification (Commentary)

Purification (Comment) Organism
purification and refolding of C-RsmC from inclusion bodies Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanine1207 in 16S rRNA
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Escherichia coli S-adenosyl-L-homocysteine + N2-methylguanine1207 in 16S rRNA
-
?

Synonyms

Synonyms Comment Organism
RsmC
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Escherichia coli