Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.174 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)

EC Number Crystallization (Comment) Organism
2.1.1.174 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

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.174 Escherichia coli P42596 gene rlmG
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.174 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)

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

Subunits

EC Number Subunits Comment Organism
2.1.1.174 monomer monomer status of RlmG in solution Escherichia coli
2.1.1.174 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

EC Number Synonyms Comment Organism
2.1.1.174 23S rRNA methyltransferase
-
 Escherichia coli
2.1.1.174 m2G1835
-
 Escherichia coli
2.1.1.174 RlmG
-
 Escherichia coli

Cofactor

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

General Information

EC Number General Information Comment Organism
2.1.1.174 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
2.1.1.174 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