X-ray diffraction
2.5Å resolution

Crystal structure of tRNA guanine-n1-methyltransferase from Bartonella henselae using MPCS.

Source organism: Bartonella henselae
Entry authors: Edwards TE, Stahl G, Gerdts CJ, Staker BL, Accelerated Technologies Center for Gene to 3D Structure (ATCG3D), Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
tRNA (guanine-N(1)-)-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 25.58 KDa
Source organism: Bartonella henselae
Expression system: Escherichia coli
  • Canonical: Q6G1R9 (Residues: 1-232; Coverage: 100%)
Gene names: BH15820, trmD
Sequence domains: tRNA (Guanine-1)-methyltransferase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 56.017Å b: 84.467Å c: 97.192Å
α: 90° β: 90° γ: 90°
R R work R free
0.196 0.195 0.225
Expression system: Escherichia coli