› 1mb2

X-ray diffraction
2.7Å resolution

Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Tryptophan in an Open Conformation

Released:
DOI: 10.2210/pdb1mb2/pdb
PDB entry 1mb2 coloured by chain, front view.
PDB entry 1mb2 coloured by chain, side view.
PDB entry 1mb2 coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations.
Retailleau P, Huang X, Yin Y, Hu M, Weinreb V, Vachette P, Vonrhein C, Bricogne G, Roversi P, Ilyin V, Carter CW
J Mol Biol 325 39-63 (2003)
PMID: 12473451

Function and Biology Details

Reaction catalysed: 
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan--tRNA ligase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 328 amino acids
Theoretical weight: 37.23 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00953 (Residues: 1-328; Coverage: 100%)
Gene name: trpS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand TRP 6 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 228.73Å b: 92.24Å c: 157.59Å
α: 90° β: 132.71° γ: 90°
R-values:
R R work R free
0.22 0.22 0.254
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Prospects for aminoacyl-tRNA synthetase inhibitors as new antimicrobial agents.
Hurdle et al. (2005)
3 more

13 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
12 more