› 2g36

X-ray diffraction
2.5Å resolution

Crystal structure of Tryptophanyl-tRNA synthetase (EC 6.1.1.2) (Tryptophan-tRNA ligase)(TrpRS) (tm0492) from THERMOTOGA MARITIMA at 2.50 A resolution

Released:
DOI: 10.2210/pdb2g36/pdb
PDB entry 2g36 coloured by chain, front view.
PDB entry 2g36 coloured by chain, side view.
PDB entry 2g36 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster.
Han GW, Yang XL, McMullan D, Chong YE, Krishna SS, Rife CL, Weekes D, Brittain SM, Abdubek P, Ambing E, Astakhova T, Axelrod HL, Carlton D, Caruthers J, Chiu HJ, Clayton T, Duan L, Feuerhelm J, Grant JC, Grzechnik SK, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kumar A, Marciano D, Miller MD, Morse AT, Nigoghossian E, Okach L, Paulsen J, Reyes R, van den Bedem H, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Elsliger MA, Schimmel P, Wilson IA
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 1326-34 (2010)
PMID: 20944229

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194556 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 39.28 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYW2 (Residues: 1-328; Coverage: 100%)
Gene names: TM_0492, trpS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SF4 1 x SF4
Ligand TRP 1 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: C2221
Unit cell:
a: 122.89Å b: 152.73Å c: 53.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.256
Expression system: Escherichia coli

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Citations

2 review citations

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Eijgenraam et al. (2018)
1 more

8 mentions without citation

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Keller et al. (2015)
7 more