› 4fno

X-ray diffraction
2.25Å resolution

Crystal structure of peptidyl t-RNA hydrolase from Pseudomonas aeruginosa at 2.2 Angstrom resolution

Released:
DOI: 10.2210/pdb4fno/pdb
PDB entry 4fno coloured by chain, front view.
PDB entry 4fno coloured by chain, side view.
PDB entry 4fno coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structural and binding studies of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa provide a platform for the structure-based inhibitor design against peptidyl-tRNA hydrolase.
Singh A, Kumar A, Gautam L, Sharma P, Sinha M, Bhushan A, Kaur P, Sharma S, Arora A, Singh TP
Biochem J 463 329-37 (2014)
PMID: 25101795

Function and Biology Details

Reaction catalysed: 
N-substituted aminoacyl-tRNA + H(2)O = N-substituted amino acid + tRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191005 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-tRNA hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 194 amino acids
Theoretical weight: 20.83 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HVC3 (Residues: 1-194; Coverage: 100%)
Gene names: PA4672, pth
Sequence domains: Peptidyl-tRNA hydrolase
Structure domains: Peptidyl-tRNA hydrolase

Ligands and Environments

2 bound ligands:
Ligand PEG 2 x PEG
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P61
Unit cell:
a: 62.604Å b: 62.604Å c: 155.392Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.205 0.251
Expression system: Escherichia coli

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Citations

8 citation in other articles

Miscoding-induced stalling of substrate translocation on the bacterial ribosome.
Alejo et al. (2017)
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2 mentions without citation

Nectin ectodomain structures reveal a canonical adhesive interface.
Harrison et al. (2012)
1 more