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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.186 - 23S rRNA (cytidine2498-2'-O)-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P0ADR6

for references in articles please use BRENDA:EC2.1.1.186
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0ADR6 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
rrna large subunit methyltransferase m, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2O-ribose methyltransferase
-
rRNA large subunit methyltransferase M
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (cytidine2498-2?-O)-methyltransferase
-
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 + cytidine2498 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine2498 in 23S rRNA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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 + cytidine2498 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine2498 in 23S rRNA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the catalytic domain of RlmM is closely related to YiiB, TlyA and fibrillarins, with the second K of the catalytic tetrad KDKE shifted by two residues at the C-terminal end of a beta strand compared with most 2'O MTases
malfunction
C2498 methylation and the putative second methylation observed in the wild-type (YgdE+) strain are completely absent in the DygdE strain. Inactivation of the ygdE gene leads to loss of methylation at nucleotide C2498. The loss of ygdE function causes a slight reduction in bacterial fitness
physiological function
RlmM catalyzes the S-adenosyl methionine-dependent 20O methylation of C2498 in 23S ribosomal RNA of Escherichia coli
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
RlmM consists of an N-terminal THUMP domain and a C-terminal catalytic Rossmann-like fold MTase domain in a distinct arrangement, detailed structure analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, using 16% (w/v) polyethylene glycol 3350, 0.05 M citric acid, 0.05 M bis-tris propane pH 5.0
purified recombinant His-tagged RlmM free or in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, 0.0015 ml 10 mg/ml protein solution os mixed with 0.0015 ml of reservoir solution containing 0.3 M ammonium tartrate, pH 7.0, and 20% PEG 3350, 20°C, 1 week, two crystal forms, X-ray diffraction structure determination and analysis at 1.9 A and 2.6 A resolution, respectively, molecular replacement
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Na2SO4 gives the highest thermal stability to RlmM
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-nitrilotriacetic acid resin column chromatography, heparin column chromatography, and Superdex 75 gel filtration
recombinant His-tagged RlmM from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) Star cells
gene rlmM, expression of His-tagged RlmM in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Purta, E.; O'Connor, M.; Bujnicki, J.M.; Douthwaite, S.
YgdE is the 2'-O-ribose methyltransferase RlmM specific for nucleotide C2498 in bacterial 23S rRNA
Mol. Microbiol.
72
1147-1158
2009
Escherichia coli (P0ADR6), Escherichia coli
Manually annotated by BRENDA team
Punekar, A.S.; Shepherd, T.R.; Liljeruhm, J.; Forster, A.C.; Selmer, M.
Crystal structure of RlmM, the 2O-ribose methyltransferase for C2498 of Escherichia coli 23S rRNA
Nucleic Acids Res.
40
10507-10520
2012
Escherichia coli (P0ADR6), Escherichia coli BW25113 (P0ADR6)
Manually annotated by BRENDA team
Guo, H.Y.; Gao, Z.Q.; Zhang, H.; Wei, Y.; Xu, J.H.; Wang, W.Y.; Yan, A.X.; Dong, Y.H.
Purification, crystallization and preliminary crystallographic analysis of the 23S rRNA methyltransferase RlmM (Cm2498) from Escherichia coli
Acta Crystallogr. Sect. F
69
640-642
2013
Escherichia coli (P0ADR6)
Manually annotated by BRENDA team