› 7wpl

X-ray diffraction
2.5Å resolution

Methionyl-tRNA synthetase from Staphylococcus aureus complexed with ATP

Released:
DOI: 10.2210/pdb7wpl/pdb
Model geometry
Fit model/data
PDB entry 7wpl coloured by chain, front view.
PDB entry 7wpl coloured by chain, side view.
PDB entry 7wpl coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus COL
Primary publication:
Fragment screening and structural analyses highlight the ATP-assisted ligand binding for inhibitor discovery against type 1 methionyl-tRNA synthetase.
Yi J, Cai Z, Qiu H, Lu F, Luo Z, Chen B, Gu Q, Xu J, Zhou H
OpenAccess logo Nucleic Acids Res (2022)
PMID: 35474479

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-177207 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 530 amino acids
Theoretical weight: 61.1 KDa
Source organism: Staphylococcus aureus subsp. aureus COL
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5HII6 (Residues: 2-520; Coverage: 79%)
Gene names: SACOL0533, metG
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 1 x ATP
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 59.657Å b: 69.251Å c: 118.033Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.224 0.271
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening.
Xiang et al. (2023)

1 mention without citation

Fragment screening and structural analyses highlight the ATP-assisted ligand binding for inhibitor discovery against type 1 methionyl-tRNA synthetase.
Yi et al. (2022)