› 1li7

X-ray diffraction
2.6Å resolution

Crystal Structure of Cysteinyl-tRNA Synthetase with Cysteine Substrate Bound

Released:
DOI: 10.2210/pdb1li7/pdb
PDB entry 1li7 coloured by chain, front view.
PDB entry 1li7 coloured by chain, side view.
PDB entry 1li7 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase.
Newberry KJ, Hou YM, Perona JJ
EMBO J 21 2778-87 (2002)
PMID: 12032090

Function and Biology Details

Reaction catalysed: 
ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149465 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 52.27 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P21888 (Residues: 1-461; Coverage: 100%)
Gene names: JW0515, b0526, cysS
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand CYS 2 x CYS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P41212
Unit cell:
a: 118.98Å b: 118.98Å c: 143.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.25 0.29
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria.
Newton et al. (2008)
7 more

6 mentions without citation

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