› 3lhd

X-ray diffraction
2.59Å resolution

Crystal structure of P. abyssi tRNA m1A58 methyltransferase in complex with S-adenosyl-L-homocysteine

Released:
DOI: 10.2210/pdb3lhd/pdb
PDB entry 3lhd coloured by chain, front view.
PDB entry 3lhd coloured by chain, side view.
PDB entry 3lhd coloured by chain, top view.
Source organism: Pyrococcus abyssi GE5
Primary publication:
Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase.
Guelorget A, Roovers M, Guérineau V, Barbey C, Li X, Golinelli-Pimpaneau B
Nucleic Acids Res 38 6206-18 (2010)
PMID: 20483913

Function and Biology Details

Reaction catalysed: 
2 S-adenosyl-L-methionine + adenine(57)/adenine(58) in tRNA = 2 S-adenosyl-L-homocysteine + N(1)-methyladenine(57)/N(1)-methyladenine(58) in tRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase TrmI Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 253 amino acids
Theoretical weight: 28.92 KDa
Source organism: Pyrococcus abyssi GE5
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9V1J7 (Residues: 1-253; Coverage: 100%)
Gene names: PAB0283, PYRAB04300, pimT-like, trmI
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 4 x SAH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 66.03Å b: 127.577Å c: 151.396Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.231 0.286
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Methylated nucleosides in tRNA and tRNA methyltransferases.
Hori H. (2014)
5 more

1 mention without citation

Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions.
Guelorget et al. (2011)