2.1.1.170: 16S rRNA (guanine527-N7)-methyltransferase

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For detailed information about 16S rRNA (guanine527-N7)-methyltransferase, go to the full flat file.

Reaction

Synonyms

16S rRNA methyltransferase, 16S rRNA methyltransferase RsmG, gidB, glucose-inhibited division protein B, ribosomal RNA small subunit methyltransferase G, rsmG, RsmG methyltransferase

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.170 16S rRNA (guanine527-N7)-methyltransferase

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Results	in table
1	Activating Compound
15708	AA Sequence
5	Cloned(Commentary)
2	Cofactor
2	Crystallization (Commentary)
2	Expression
14	General Information
1	Metals/Ions
2	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
146	Organism
1	pH Optimum
19	Protein Variants
3	Purification (Commentary)
1	Reaction
13	Reference
1	Source Tissue
13	Substrates and Products (Substrate)
1	Subunits
19	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]

Crystallization

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Crystallization on EC 2.1.1.170 - 16S rRNA (guanine527-N7)-methyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting-drop vapor diffusion at 4°C against a reservoir containing 0.1 M of sodium citrate pH 6.5, 15% polyethylene glycol 4000, and 10% isopropanol

Escherichia coli

P0A6U5

706646

microbatch technique under oil at 4°C. Determination of the structure of RsmG (249 amino acids) in three different crystal forms: the enzyme in complex with the cofactor S-adensosyl-L-methionine, the enzyme in complex with S-adenosyl-L-homocysteine, the enzyme in complex with adenosine monophosphate and S-adenosyl-L-methionine. RsmG X-ray crystal structures at up to 1.5 A resolution. Cofactor-bound crystal structures of RsmG reveals a positively charged surface area remote from the active site that binds an adenosine monophosphate molecule

Thermus thermophilus

Q9LCY2

706725