› 7o4m

X-ray diffraction
1.3Å resolution

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + adenine(22) in tRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(22) in tRNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101144 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA (Adenine-N(1))-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 25.59 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0D6HIR7 (Residues: 1-225; Coverage: 100%)
Gene names: ACR74_00680, C0102_07490, CNH36_08360, EIG96_09170, EP54_01080, EQ90_01915, GO814_12715, GO942_05350, GQX37_09795, HMPREF3211_01711, LB359_02015, NCTC13131_01930, SAMEA1029512_00536, SAMEA1029528_01600, SAMEA1029536_00496, SAMEA2078260_01295, SAMEA2078588_01404, SAMEA2080344_01594, SAMEA2081063_01144, SAMEA4008575_01427, SAMEA70146418_01109, trmK
Sequence domains: tRNA (adenine(22)-N(1))-methyltransferase

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 59.225Å b: 60.705Å c: 63.128Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.116 0.115 0.148
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Application of mutational profiling: New functional analyses reveal the tRNA recognition mechanism of tRNA m1A22 methyltransferase.
Yamagami et al. (2023)
1 more

1 mention without citation

Structure, dynamics, and molecular inhibition of the Staphylococcus aureus m1A22-tRNA methyltransferase TrmK.
Sweeney et al. (2022)