› 3h9c

X-ray diffraction
1.4Å resolution

Structure of methionyl-tRNA synthetase: crystal form 2

Released:
DOI: 10.2210/pdb3h9c/pdb
PDB entry 3h9c coloured by chain, front view.
PDB entry 3h9c coloured by chain, side view.
PDB entry 3h9c 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: 547 amino acids
Theoretical weight: 62.47 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00959 (Residues: 2-548; Coverage: 81%)
Gene names: JW2101, b2114, metG
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 78.89Å b: 45.4Å c: 86.21Å
α: 90° β: 107.3° γ: 90°
R-values:
R R work R free
0.167 0.165 0.191
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

3 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
2 more