Literature summary for 2.1.1.174 extracted from

Zhang, H.; Gao, Z.Q.; Wei, Y.; Wang, W.J.; Liu, G.F.; Shtykova, E.V.; Xu, J.H.; Dong, Y.H.
Structural insights into the function of 23S rRNA methyltransferase RlmG (m2G1835) from Escherichia coli (2012), RNA, 18, 1500-1509.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of C-terminally His6-tagged full-length enzyme, expression of the C-terminal domain and the N-terminal domain as SUMO fusion proteins, the C-terminal domain is unstable after detagging through ubiquitin-like-specific protease 1 cleavage, while the N-terminal domain is stable	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
RlmG in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, room temperature, mixture of RlmG with S-adenosyl-L-methionine in solution 0.2 M Tris, pH 7.5, and 5% w/v PEG 8000 with the addition of 1% w/v protamine sulfate, and 0.02 M HEPES sodium, pH 6.8, 3-4 days, X-ray diffraction structure determination and analysis at 2.3 A resolution, single-wavelength anomalous dispersion	Escherichia coli

Crystallization (Comment)

Organism

RlmG in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, room temperature, mixture of RlmG with S-adenosyl-L-methionine in solution 0.2 M Tris, pH 7.5, and 5% w/v PEG 8000 with the addition of 1% w/v protamine sulfate, and 0.02 M HEPES sodium, pH 6.8, 3-4 days, X-ray diffraction structure determination and analysis at 2.3 A resolution, single-wavelength anomalous dispersion

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of two deletion mutants corresponding to the isolated N-terminal domain and C-terminal domain	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Escherichia coli	molecular modeling of RlmG-AdoMet-rRNA complex	?	-	?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA	Escherichia coli	-	S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P42596	gene rlmG	-

Reaction

Reaction	Comment	Organism	Reaction ID
S-adenosyl-L-methionine + guanine1835 in 23S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA	catalytic mechanism, overview	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	molecular modeling of RlmG-AdoMet-rRNA complex	Escherichia coli	?	-	?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA	-	Escherichia coli	S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA	-	?

Subunits

Subunits	Comment	Organism
monomer	monomer status of RlmG in solution	Escherichia coli
More	RlmG possesses two homologous domains: the N-terminal domain in the recognition and binding of the substrate, and the C-terminal domain in S-adenosyl-L-methionine-binding and the catalytic process. The N-terminal domain can bind RNA independently and RNA binding is achieved by the N-terminal domain, accomplished by a coordinating role of the C-terminal domain	Escherichia coli

Synonyms

Synonyms	Comment	Organism
23S rRNA methyltransferase	-	Escherichia coli
m2G1835	-	Escherichia coli
RlmG	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	binds in the active site of the C-terminal domain, structure, overview	Escherichia coli

General Information

General Information	Comment	Organism
additional information	RlmG possesses two homologous domains: the N-terminal domain in the recognition and binding of the substrate, and the C-terminal domain in S-adenosyl-L-methionine-binding and the catalytic process. The N-terminal domain can bind RNA independently and RNA binding is achieved by the N-terminal domain, accomplished by a coordinating role of the C-terminal domain, modeling of the RlmG-AdoMet-RNA complex, overview. RlmG may unfold its substrate RNA in the positively charged cleft between the NTD and CTD, and then G1835 disengages from its Watson-Crick pairing with C1905 and flips out to insert into the active site	Escherichia coli
physiological function	RlmG is a specific S-adenosyl-L-methionine-dependent methyltransferase responsible for N2-methylation of G1835 in 23S rRNA of Escherichia coli. Methylation of m2G1835 specifically enhances association of ribosomal subunits and provides a significant advantage for bacteria in osmotic and oxidative stress	Escherichia coli