› 1rqg

X-ray diffraction
2.9Å resolution

Methionyl-tRNA synthetase from Pyrococcus abyssi

Released:
DOI: 10.2210/pdb1rqg/pdb
PDB entry 1rqg coloured by chain, front view.
PDB entry 1rqg coloured by chain, side view.
PDB entry 1rqg coloured by chain, top view.
Source organism: Pyrococcus abyssi
Primary publication:
Three-dimensional structure of methionyl-tRNA synthetase from Pyrococcus abyssi.
Crepin T, Schmitt E, Blanquet S, Mechulam Y
Biochemistry 43 2635-44 (2004)
PMID: 14992601

Function and Biology Details

Reaction catalysed: 
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194149 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 722 amino acids
Theoretical weight: 84.43 KDa
Source organism: Pyrococcus abyssi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9V011 (Residues: 1-722; Coverage: 100%)
Gene names: PAB2364, PYRAB09870, metG, metS
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: I4122
Unit cell:
a: 113.15Å b: 113.15Å c: 287.016Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.244 0.297
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Emergence and evolution.
Bullwinkle et al. (2014)
1 more

1 mention without citation

Exploring Proteus mirabilis Methionine tRNA Synthetase Active Site: Homology Model Construction, Molecular Dynamics, Pharmacophore and Docking Validation.
Elbaramawi et al. (2023)