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Information on EC 2.1.1.217 - tRNA (adenine22-N1)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.217
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.217 tRNA (adenine22-N1)-methyltransferase
IUBMB Comments
The enzyme specifically methylates adenine22 in tRNA.
The enzyme appears in viruses and cellular organisms
- 2.1.1.217
- mtases
- methyltransferases
- adomet
-
rna-binding
-
groove
-
sam-dependent
-
class-i
-
ligand-free
Reaction Schemes
show+
adenine22 in tRNA
=
+
N1-methyladenine22 in tRNA
Synonyms
bstrmk, class i mtase, sp1610, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BsTrmK
EC 2.1.1.36
-
-
formerly, part transferred
-
m1A22 MTase
m1A22 tRNA methyltransferase
TrmK
yqfN
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + adenine22 in tRNA = S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (adenine22-N1)-methyltransferase
The enzyme specifically methylates adenine22 in tRNA.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + adenine22 in Bacillus subtilis tRNA(Ser)
S-adenosyl-L-homocysteine + N1-methyladenine22 in Bacillus subtilis tRNA(Ser)
Substrates: crude Escherichia coli tRNA is used, since it does not contain m1A22
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
S-adenosyl-L-methionine + adenine22 in tRNALeu
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNALeu
Substrates: adenine at position 22 of tRNALeu is absolutely essential. Variants carrying C, U or G in position 22 are no substrates
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
S-adenosyl-L-methionine + adenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: a methyl group at position N1 prevents Watson-Crick-type base pairing by adenosine and is therefore important for regulation of structure and stability of tRNA molecules
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: crude Escherichia coli tRNA is used, since it does not contain m1A22
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
A0A0E1R6X8
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
A0A0E1R6X8
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
Substrates: interaction of BstRNASer with BsTrmK/SAH is deciphered by NMR. The tRNASer produced in Escherichia coli is less efficiently modified than the unmodified tRNASer
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
Substrates: interaction of BstRNASer with BsTrmK/SAH is deciphered by NMR. The tRNASer produced in Escherichia coli is less efficiently modified than the unmodified tRNASer
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
Products: -
Products: -
?
additional information
?
-
-
Substrates: the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
Products: -
Products: -
?
additional information
?
-
Substrates: the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
Products: -
Products: -
?
additional information
?
-
Substrates: an RNA18mer, predicted to form a hairpin similar to the D-arm of tRNA but with only four nucleotides in the loop and containing adenine at three positions, is accepted as substrate
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: a methyl group at position N1 prevents Watson-Crick-type base pairing by adenosine and is therefore important for regulation of structure and stability of tRNA molecules
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
A0A0E1R6X8
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
A0A0E1R6X8
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
S-adenosyl-L-homocysteine binding leads to an entropic penalty compensated for by a large favorable enthalpic contribution
-
S-adenosyl-L-methionine
SAM, enzyme binding structure analysis, overview. SAM is modelled into the active site of BsTrmK, guided by the crystal structure of SAM-bound TrmK from Streptomyces pneumoniae (PDB ID 3KU1). The SAM cofactor is bound at the centre of the catalytic domain in a pocket with residues harbouring negative electrostatic potentials conserved amongst COG2384 proteins. The methyl group is pointing towards a region of positively charged and well conserved residues, likely important for tRNA binding
S-adenosyl-L-methionine
SAM binds to the enzyme with favorable but modest enthalpic and entropic contributions. SAM binding to the N-terminal domain alters specific motions of the C-terminal domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Plumbagin
protein is covalently modified at residue C92 by one equivalent of the inhibitor
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
the higher oligomeric states of BsTrmK are formed via disulphide bonds involving the two cysteines in BsTrmK sequence at positions 35 and 152. Such bonds can be broken by addition of a reducing-agent, and addition of DTT to the MTase reaction buffer results in a dramatic increase of the enzymatic activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
[Comparative study of the tRNA-methylases of normal and tumor tissues. II. Positional specificity of renal and carcinoma RA methylases]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000042
adenine22 in tRNASer
recombinant enzyme, pH 8.0, 37°C, in vitro activity
-
0.000079
adenine22 in tRNASer
recombinant enzyme, pH 8.0, 37°C, in vivo activity
-
additional information
additional information
Michaelis-Menten kinetics, steady-state kinetic analysis of BsTrmK
-
additional information
additional information
-
Michaelis-Menten kinetics, steady-state kinetic analysis of BsTrmK
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
Bacillus subtilis TrmK belongs to the COG2384 (cluster of orthologous groups). The members of this family are found in Gram-negative and Gram-positive bacteria. Their sequences are well-conserved in many bacterial pathogens
evolution
-
the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
evolution
the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
evolution
A0A0E1R6X8
the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
evolution
the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
evolution
-
Bacillus subtilis TrmK belongs to the COG2384 (cluster of orthologous groups). The members of this family are found in Gram-negative and Gram-positive bacteria. Their sequences are well-conserved in many bacterial pathogens
-
evolution
-
the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
-
metabolism
-
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
metabolism
A0A0E1R6X8
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
metabolism
-
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
-
physiological function
-
the enzyme is essential for the bacterial survival
physiological function
the enzyme is essential for the bacterial survival
physiological function
A0A0E1R6X8
the enzyme is essential for the bacterial survival
physiological function
the enzyme is essential for the bacterial survival
physiological function
-
the enzyme is essential for the bacterial survival
-
additional information
NMR chemical shift mapping is used to get insight on the protein-RNA recognition mode
additional information
-
NMR chemical shift mapping is used to get insight on the protein-RNA recognition mode
additional information
the crystal structure of BsTrmK shows an N-terminal catalytic domain harbouring the typical Rossmann-like fold of Class-I methyltransferases and a C-terminal coiled-coil domain. Docking of BstRNASer to BsTrmK in complex with its methyldonor cofactor S-adenosyl-L-methionine (SAM) by NMR chemical shift mapping, modelling, overview. Both domains of BsTrmK participate in tRNA binding. BsTrmK recognises tRNA with very few structural changes in both partner, the non-Watson-Crick R13-A22 base-pair positioning the A22 N1-atom close to the SAM methyl group. BsTrmK requires the intact three-dimensional structure of tRNA to catalyse m1A22 formation
additional information
-
the crystal structure of BsTrmK shows an N-terminal catalytic domain harbouring the typical Rossmann-like fold of Class-I methyltransferases and a C-terminal coiled-coil domain. Docking of BstRNASer to BsTrmK in complex with its methyldonor cofactor S-adenosyl-L-methionine (SAM) by NMR chemical shift mapping, modelling, overview. Both domains of BsTrmK participate in tRNA binding. BsTrmK recognises tRNA with very few structural changes in both partner, the non-Watson-Crick R13-A22 base-pair positioning the A22 N1-atom close to the SAM methyl group. BsTrmK requires the intact three-dimensional structure of tRNA to catalyse m1A22 formation
additional information
-
NMR chemical shift mapping is used to get insight on the protein-RNA recognition mode
-
additional information
-
the crystal structure of BsTrmK shows an N-terminal catalytic domain harbouring the typical Rossmann-like fold of Class-I methyltransferases and a C-terminal coiled-coil domain. Docking of BstRNASer to BsTrmK in complex with its methyldonor cofactor S-adenosyl-L-methionine (SAM) by NMR chemical shift mapping, modelling, overview. Both domains of BsTrmK participate in tRNA binding. BsTrmK recognises tRNA with very few structural changes in both partner, the non-Watson-Crick R13-A22 base-pair positioning the A22 N1-atom close to the SAM methyl group. BsTrmK requires the intact three-dimensional structure of tRNA to catalyse m1A22 formation
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A0H2UR54_STRPN
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
225
0
24936
TrEMBL
-
A0A0C3A3T0_MYCCA
225
0
26339
TrEMBL
Secretory Pathway (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
BsTrmK is active as a monomer, the higher oligomeric states of BsTrmK are formed via disulphide bonds involving the two cysteines in BsTrmK sequence at positions 35 and 152. Such bonds can be broken by addition of a reducing-agent, and addition of DTT to the MTase reaction buffer results in a dramatic increase of the enzymatic activity
monomer
-
BsTrmK is active as a monomer, the higher oligomeric states of BsTrmK are formed via disulphide bonds involving the two cysteines in BsTrmK sequence at positions 35 and 152. Such bonds can be broken by addition of a reducing-agent, and addition of DTT to the MTase reaction buffer results in a dramatic increase of the enzymatic activity
-
monomer
1 * 25564.5, (ESI)/TOF-MS, 1 * 25565.3, calculated from sequence
monomer
Sp1610 exists as a monomer both in solution and in the P212121 crystal
additional information
backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
additional information
-
backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
additional information
BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
additional information
-
BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
additional information
-
backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
-
additional information
-
BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, mixing of 0.0016 ml of 3 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 500 mM NaCl, and 2% glycerol, with crystallization solution containing 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate, pH 5.0, 30% w/v PEG 4000, and 8% 2-methyl-2,4-pentanediol, and equuilibration against 0.1 ml reservoir solution, microseeding, 4°C, X-ray diffraction structure determination and analysis, molecular replacement using structures of sp1610 (Streptococcus pneumoniae orthologue of BsTrmK, PDB code 3KR9), LMOf2365 1472 (Listeria Monocytogens, PDB code 3GNL) and of SAG1203 (Streptococcus agalactiae, PDB code: 3LEC) as templates, modelling
structures of TrmK apoenzyme and in complexes with SAM and SAH, to 1.3, 1.4, and 1.5 A resolution, respectively
crystal structure of Sp1610 in the ligand-free and the AdoMet-bound forms at resolutions of 2.0 and 3.0 A, microbatch method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C35S/C152S
C35S/C152S
site-directed mutagenesis, since wild-type TrmK is prone to aggregation through cysteine oxidation, a protein variant with cysteine to serine mutations (i.e. C35S and C152S) is produced, which shows abolished protein aggregation and retains full enzymatic activity
C35S/C152S
-
site-directed mutagenesis, since wild-type TrmK is prone to aggregation through cysteine oxidation, a protein variant with cysteine to serine mutations (i.e. C35S and C152S) is produced, which shows abolished protein aggregation and retains full enzymatic activity
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged mutant enzyme C35S/C152S from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, followed by ultrafiltration and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene trmK, recombinant overexpression of N-terminally His6-tagged mutant enzyme C35S/C152S in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roovers, M.; Kaminska, K.H.; Tkaczuk, K.L.; Gigot, D.; Droogmans, L.; Bujnicki, J.M.
The YqfN protein of Bacillus subtilis is the tRNA: m1A22 methyltransferase (TrmK)
Nucleic Acids Res.
36
3252-3262
2008
Bacillus subtilis (P54471), Bacillus subtilis
brenda
Ta, H.M.; Kim, K.K.
Crystal structure of Streptococcus pneumoniae Sp1610, a putative tRNA methyltransferase, in complex with S-adenosyl-L-methionine
Protein Sci.
19
617-624
2010
Streptococcus pneumoniae (A0A0H2UR54), Streptococcus pneumoniae
brenda
Degut, C.; Barraud, P.; Larue, V.; Tisne, C.
Backbone resonance assignments of the m1A22 tRNA methyltransferase TrmK from Bacillus subtilis
Biomol. NMR Assign.
10
253-257
2016
Bacillus subtilis (P54471), Bacillus subtilis, Bacillus subtilis 168 (P54471)
brenda
Oerum, S.; Degut, C.; Barraud, P.; Tisne, C.
m1A Post-transcriptional modification in tRNAs
Biomolecules
7
20
2017
Listeria monocytogenes serotype 4b (A0A0E1R6X8), Listeria monocytogenes serotype 4b LL195 (A0A0E1R6X8), Staphylococcus aureus (A0A0D6HIR7), Streptococcus pneumoniae, Vibrio cholerae (A0A0H6U323)
brenda
Degut, C.; Roovers, M.; Barraud, P.; Brachet, F.; Feller, A.; Larue, V.; Al Refaii, A.; Caillet, J.; Droogmans, L.; Tisne, C.
Structural characterization of B. subtilis m1A22 tRNA methyltransferase TrmK insights into tRNA recognition
Nucleic Acids Res.
47
4736-4750
2019
Bacillus subtilis (P54471), Bacillus subtilis, Bacillus subtilis 168 (P54471), no activity in Escherichia coli
brenda
Sweeney, P.; Galliford, A.; Kumar, A.; Raju, D.; Krishna, N.; Sutherland, E.; Leo, C.; Fisher, G.; Lalitha, R.; Muthuraj, L.; Sigamani, G.; Oehler, V.; Synowsky, S.; Shirran, S.; Gloster, T.; Czekster, C.; Kumar, P.; da Silva, R.
Structure, dynamics, and molecular inhibition of the Staphylococcus aureus m1A22-tRNA methyltransferase TrmK
J. Biol. Chem.
298
102040
2022
Staphylococcus aureus (A0A0D6HIR7)
brenda
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