› 1pfv

X-ray diffraction
1.7Å resolution

METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH DIFLUOROMETHIONINE

Released:
DOI: 10.2210/pdb1pfv/pdb
PDB entry 1pfv coloured by chain, front view.
PDB entry 1pfv coloured by chain, side view.
PDB entry 1pfv coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase.
Crepin T, Schmitt E, Mechulam Y, Sampson PB, Vaughan MD, Honek JF, Blanquet S
J Mol Biol 332 59-72 (2003)
PMID: 12946347

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-524479 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 551 amino acids
Theoretical weight: 62.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00959 (Residues: 2-552; Coverage: 81%)
Gene names: JW2101, b2114, metG
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand 2FM 1 x 2FM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 78.573Å b: 45.221Å c: 86.068Å
α: 90° β: 107.37° γ: 90°
R-values:
R R work R free
0.186 0.186 0.203
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Geometry of nonbonded interactions involving planar groups in proteins.
Chakrabarti et al. (2007)
3 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)