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Information on EC 2.1.1.170 - 16S rRNA (guanine527-N7)-methyltransferase and Organism(s) Thermus thermophilus and UniProt Accession Q9LCY2

for references in articles please use BRENDA:EC2.1.1.170
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IUBMB Comments
The enzyme specifically methylates guanine527 at N7 in 16S rRNA.
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q9LCY2
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The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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S-adenosyl-L-methionine
+
guanine527 in 16S rRNA
=
S-adenosyl-L-homocysteine
+
N7-methylguanine527 in 16S rRNA
+
guanine527 in 16S rRNA
=
+
N7-methylguanine527 in 16S rRNA
Synonyms
16s rrna methyltransferase, ribosomal rna small subunit methyltransferase g, rsmg methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16S rRNA methyltransferase RsmG
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ribosomal RNA small subunit methyltransferase G
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine527-N7)-methyltransferase
The enzyme specifically methylates guanine527 at N7 in 16S rRNA.
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 + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S 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 + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
show the reaction diagram
methylations concentrated in the decoding site of the 30S ribosomal subunit may act to fine tune codon recognition in a manner similar to tRNA modifications. The intact 30S subunit is very unlikely to be the natural substrate for Thermus thermophilus RsmG in vivo. This interpretation is consistent with the position of G527 in the intact 30S subunit, where it is buried and would be inaccessible for methylation without substantial unfolding of the local subunit structure. Deproteinized 16S rRNA is the most active substrate in vitro. In vivo, several ribosomal proteins probably begin binding to the nascent 16S rRNA transcript prior to its completion, making an early assembly intermediate a plausible candidate for the biological substrate of RsmG
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
S-adenosyl-L-methionine is bound in a canonical conformation above the beta-sheet and close to the conserved GxGxG methyltransferase signature motif (residues 88–92 between strand beta1 and helix alpha4). The AdoMet cofactor is tightly bound in RsmG and copurifies with the recombinant protein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the 30S subunits in their native conformation are not a proper substrate and removal of Mg2+ ions from the subunit is required to open the structure sufficiently to expose elements involved in enzyme binding
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
construction of an rsmG null allele by deleting the rsmG coding sequence and replacing it with htk, encoding a heat-stable kanamycin adenyltransferase. This null allele retains the very N- and C-terminal rsmG coding sequences, in-frame with the htk coding sequence, in order to maintain the rsmG–parA overlap and minimize any effects on parA expression. This allele is designated DrsmGThtk2 and the mutant containing this allele is designated HG 917. Thermus thermophilus rsmG mutants are weakly resistant to the aminoglycoside antibiotic streptomycin. Growth competition experiments indicate a physiological cost to loss of RsmG activity, consistent with the conservation of the modification site in the decoding region of the ribosome
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch technique under oil at 4°C. Determination of the structure of RsmG (249 amino acids) in three different crystal forms: the enzyme in complex with the cofactor S-adensosyl-L-methionine, the enzyme in complex with S-adenosyl-L-homocysteine, the enzyme in complex with adenosine monophosphate and S-adenosyl-L-methionine. RsmG X-ray crystal structures at up to 1.5 A resolution. Cofactor-bound crystal structures of RsmG reveals a positively charged surface area remote from the active site that binds an adenosine monophosphate molecule
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the AdoMet cofactor is tightly bound in RsmG and copurifies with the recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gregory, S.T.; Demirci, H.; Belardinelli, R.; Monshupanee, T.; Gualerzi, C.; Dahlberg, A.E.; Jogl, G.
Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG
RNA
15
1693-1704
2009
Thermus thermophilus (Q9LCY2), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q9LCY2)
Manually annotated by BRENDA team