Literature summary for 2.1.1.199 extracted from

Wei, Y.; Zhang, H.; Gao, Z.Q.; Wang, W.J.; Shtykova, E.V.; Xu, J.H.; Liu, Q.S.; Dong, Y.H.
Crystal and solution structures of methyltransferase RsmH provide basis for methylation of C1402 in 16S rRNA (2012), J. Struct. Biol., 179, 29-40.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene rsmH, expression of His6-tagged RsmH in Escherichia coli strain BL21 DE3 star	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His6-tagged RsmH in complex with S-adenosyl-L-methionine and cytidine in a 1:5:5 ratio, sitting drop vapour diffusion method, from 20 mM Tris, 100 mM NaCl, 5% v/v glycerol, 2 mM DTT, pH 8.0, room temperature, the best crystal is obtained in the mixture solution 1.0 M ammonium sulfate, 0.1 M HEPES, pH 6.5, and 0.5% w/v PEG 8, 000 in 3-4 days, X-ray diffraction structure determination and analysis at 2.25 A resolution	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant His6-tagged RsmH in complex with S-adenosyl-L-methionine and cytidine in a 1:5:5 ratio, sitting drop vapour diffusion method, from 20 mM Tris, 100 mM NaCl, 5% v/v glycerol, 2 mM DTT, pH 8.0, room temperature, the best crystal is obtained in the mixture solution 1.0 M ammonium sulfate, 0.1 M HEPES, pH 6.5, and 0.5% w/v PEG 8, 000 in 3-4 days, X-ray diffraction structure determination and analysis at 2.25 A resolution

Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + cytidine1402 in 16S rRNA	Escherichia coli	-	S-adenosyl-L-homocysteine + N4-methylcytidine1402 in 16S rRNA	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P60390	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged RsmH from Escherichia coli strain BL21 DE3 star by nickel affinity chromatigraphy and gel filtration	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + cytidine1402 in 16S rRNA	-	Escherichia coli	S-adenosyl-L-homocysteine + N4-methylcytidine1402 in 16S rRNA	-	?

Subunits

Subunits	Comment	Organism
homodimer	active enzyme in solution, structure analysis, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
methyltransferase RsmH	-	Escherichia coli
RsmH	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	the cofactor binds in the active site, structure, overview	Escherichia coli

General Information

General Information	Comment	Organism
additional information	RsmH in complex with S-adenosyl-L-methionine and cytidine consists of two distinct but structurally related domains: the typical MTase domain and the putative substrate recognition and binding domain. A deep pocket occurs in the conserved AdoMet binding domain, cytidine binds far from S-adenosyl-L-methionine with the distance of 25.9 A, The complex is not in a catalytically active state, and structural rearrangement of RsmH or the nucleotides neighboring C1402 may be necessary to trigger catalysis	Escherichia coli