Information on EC 2.1.1.174 - 23S rRNA (guanine1835-N2)-methyltransferase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
2.1.1.174
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RECOMMENDED NAME
GeneOntology No.
23S rRNA (guanine1835-N2)-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine1835 in 23S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (guanine1835-N2)-methyltransferase
The enzyme methylates 23S rRNA in vitro, assembled 50S subunits are not a substrate [1]. The enzyme specifically methylates guanine1835 at N2 in 23S rRNA.
CAS REGISTRY NUMBER
COMMENTARY hide
50812-26-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
show the reaction diagram
additional information
?
-
molecular modeling of RlmG-AdoMet-rRNA complex
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
show the reaction diagram
additional information
?
-
P42596
molecular modeling of RlmG-AdoMet-rRNA complex
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
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x * 71000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 71000, SDS-PAGE
monomer
monomer status of RlmG in solution
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
recombinant YgjO protein carrying a C-terminal GFP-His6-tag is expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (2566 entries)
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