› 3h99

X-ray diffraction
1.4Å resolution

Structure of a mutant methionyl-tRNA synthetase with modified specificity complexed with methionine

Released:
DOI: 10.2210/pdb3h99/pdb
PDB entry 3h99 coloured by chain, front view.
PDB entry 3h99 coloured by chain, side view.
PDB entry 3h99 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Switching from an induced-fit to a lock-and-key mechanism in an aminoacyl-tRNA synthetase with modified specificity.
Schmitt E, Tanrikulu IC, Yoo TH, Panvert M, Tirrell DA, Mechulam Y
J Mol Biol 394 843-51 (2009)
PMID: 19837083

Function and Biology Details

Reaction catalysed: 
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 560 amino acids
Theoretical weight: 63.91 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00959 (Residues: 1-548; Coverage: 81%)
Gene names: JW2101, b2114, metG
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MET 1 x MET
Ligand ZN 1 x ZN
Ligand CIT 2 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 78.172Å b: 45.293Å c: 85.967Å
α: 90° β: 107.25° γ: 90°
R-values:
R R work R free
0.168 0.168 0.18
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.
Hartman MCT. (2022)
7 other articles

1 mention without citation

Switching from an induced-fit to a lock-and-key mechanism in an aminoacyl-tRNA synthetase with modified specificity.
Schmitt et al. (2009)