› 7nu7

X-ray diffraction
2.31Å resolution

Crystal Structure of Neisseria gonorrhoeae LeuRS in Complex with ATP in Conformation 2

Released:
DOI: 10.2210/pdb7nu7/pdb
PDB entry 7nu7 coloured by chain, front view.
PDB entry 7nu7 coloured by chain, side view.
PDB entry 7nu7 coloured by chain, top view.
Source organism: Neisseria gonorrhoeae
Primary publication:
Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip.
Pang L, Zanki V, Strelkov SV, Van Aerschot A, Gruic-Sovulj I, Weeks SD
Commun Biol 5 883 (2022)
PMID: 36038645

Function and Biology Details

Reaction catalysed: 
ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110119 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 877 amino acids
Theoretical weight: 98.19 KDa
Source organism: Neisseria gonorrhoeae
Expression system: Escherichia coli
UniProt:
  • Canonical: B4RNT1 (Residues: 1-876; Coverage: 100%)
Gene names: NGK_0009, leuS
Sequence domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-3
Spacegroup: P212121
Unit cell:
a: 49.141Å b: 82.728Å c: 228.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.264
Expression system: Escherichia coli

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Citations

1 review citation

Aminoacyl tRNA Synthetases: Implications of Structural Biology in Drug Development against Trypanosomatid Parasites.
Nasim et al. (2023)
1 other article