3m5w

X-ray diffraction
2.32Å resolution

Crystal Structure of Tryptophanyl-tRNA Synthetase from Campylobacter jejuni

Released:
Entry authors: Kim Y, Zhou M, Hasseman J, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-192898 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 36.87 KDa
Source organism: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9PIB4 (Residues: 1-319; Coverage: 100%)
Gene names: Cj0388, trpS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 66.153Å b: 50.604Å c: 108.64Å
α: 90° β: 107.61° γ: 90°
R-values:
R R work R free
0.187 0.183 0.243
Expression system: Escherichia coli BL21