BRENDA - Enzyme Database
show all sequences of 2.1.1.174

Structural insights into the function of 23S rRNA methyltransferase RlmG (m2G1835) from Escherichia coli

Zhang, H.; Gao, Z.Q.; Wei, Y.; Wang, W.J.; Liu, G.F.; Shtykova, E.V.; Xu, J.H.; Dong, Y.H.; RNA 18, 1500-1509 (2012)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
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 (Commentary)
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
Engineering
Protein Variants
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
Commentary
Textmining
Escherichia coli
P42596
gene rlmG
-
Reaction
Reaction
Commentary
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
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
molecular modeling of RlmG-AdoMet-rRNA complex
721034
Escherichia coli
?
-
-
-
-
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
-
721034
Escherichia coli
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
-
-
-
?
Subunits
Subunits
Commentary
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
Commentary
Organism
23S rRNA methyltransferase
-
Escherichia coli
m2G1835
-
Escherichia coli
RlmG
-
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
binds in the active site of the C-terminal domain, structure, overview
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
binds in the active site of the C-terminal domain, structure, overview
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
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
Engineering (protein specific)
Protein Variants
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
molecular modeling of RlmG-AdoMet-rRNA complex
721034
Escherichia coli
?
-
-
-
-
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
-
721034
Escherichia coli
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
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
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
721034
Zhang
Structural insights into the f ...
Escherichia coli
RNA
18
1500-1509
2012
-
-
1
1
1
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
2
2
3
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
2
2
-
-
-
719013
Osterman
Methylated 23S rRNA nucleotide ...
Escherichia coli
Biochimie
93
725-729
2011
-
-
-
-
1
-
-
-
-
1
-
1
-
3
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
689247
Sergiev
Ribosomal RNA guanine-(N2)-met ...
Escherichia coli
Nucleic Acids Res.
35
2295-2301
2007
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
675412
Sergiev
Identification of Escherichia ...
Escherichia coli
J. Mol. Biol.
364
26-31
2006
-
-
1
-
-
-
-
-
-
-
1
1
-
2
-
-
1
-
-
-
-
-
2
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-